PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9351809-5 1997 Comparison of the bound and unbound Nef structures revealed that a proline-rich motif (Pro-x-x-Pro), which is implicated in SH3 binding, is partially disordered in the absence of the binding partner; this motif only fully adopts a left-handed polyproline type II helix conformation upon complex formation with the Fyn SH3 domain. Proline 67-74 S100 calcium binding protein B Homo sapiens 36-39 8862424-8 1996 We observe that, in addition to the membrane targeting signal and the conserved arg-arg residues within the core region, mutations in the proline-rich domain of Nef also affect its ability to associate with the serine kinase activity. Proline 138-145 S100 calcium binding protein B Homo sapiens 161-164 9288906-3 1997 This Nef/actin complex was present in human B and T lymphocytes but not in insect cells and was dependent on the N-terminal myristoylation of Nef, whereas the SH3-binding proline motif of Nef was not involved. Proline 171-178 S100 calcium binding protein B Homo sapiens 5-8 9288906-3 1997 This Nef/actin complex was present in human B and T lymphocytes but not in insect cells and was dependent on the N-terminal myristoylation of Nef, whereas the SH3-binding proline motif of Nef was not involved. Proline 171-178 S100 calcium binding protein B Homo sapiens 142-145 9288906-3 1997 This Nef/actin complex was present in human B and T lymphocytes but not in insect cells and was dependent on the N-terminal myristoylation of Nef, whereas the SH3-binding proline motif of Nef was not involved. Proline 171-178 S100 calcium binding protein B Homo sapiens 142-145 9218412-6 1997 Mutagenesis of the Nef proline-rich motif essential for SH3 binding completely blocked complex formation, kinase activation, and transformation, indicating that the Nef SH3-binding function is required for its effects on Hck. Proline 23-30 S100 calcium binding protein B Homo sapiens 19-22 9218412-6 1997 Mutagenesis of the Nef proline-rich motif essential for SH3 binding completely blocked complex formation, kinase activation, and transformation, indicating that the Nef SH3-binding function is required for its effects on Hck. Proline 23-30 S100 calcium binding protein B Homo sapiens 165-168 8794306-4 1996 A proline-rich repeat sequence [(Pxx)4] in Nef occurring between amino acid residues 69 to 78 is highly conserved and bears strong resemblance to a defined consensus sequence identified as an SH3 binding domain present in several proteins which can interact with the SH3 domain of various signalling and cytoskeletal proteins. Proline 2-9 S100 calcium binding protein B Homo sapiens 43-46 8794306-5 1996 Binding and coprecipitation assays with short synthetic peptides corresponding to the proline-rich repeat sequence [(Pxx)4] of Nef and the SH2, SH3, or SH2 and SH3 domains of Lck revealed that the interaction between these two proteins is at least in part mediated by the proline repeat sequence of Nef and the SH3 domain of Lck. Proline 272-279 S100 calcium binding protein B Homo sapiens 127-130 8794306-6 1996 In addition to direct binding to full-length Nef, MAPK was also shown to bind the same proline repeat motif. Proline 87-94 S100 calcium binding protein B Homo sapiens 45-48 8862424-11 1996 In contrast, the proline-rich region of Nef is found to be involved in mediating efficient proviral DNA synthesis and the enhanced virion-infectivity function, but is not necessary for CD4 down-modulation by Nef. Proline 17-24 S100 calcium binding protein B Homo sapiens 40-43 8862424-13 1996 These findings define three functional domains of Nef that are required for its interaction with the serine kinase activity and suggest that the cellular interaction events via the myristoylation and arg-arg regions of Nef lie upstream of the interaction event via the proline-rich domain. Proline 269-276 S100 calcium binding protein B Homo sapiens 50-53 8862424-13 1996 These findings define three functional domains of Nef that are required for its interaction with the serine kinase activity and suggest that the cellular interaction events via the myristoylation and arg-arg regions of Nef lie upstream of the interaction event via the proline-rich domain. Proline 269-276 S100 calcium binding protein B Homo sapiens 219-222 33787846-3 2021 For example, the combination of a linear proline-rich motif and hydrophobic core domain surface allows Nef to bind tightly and specifically to SH3 domains of Src family kinases. Proline 41-48 S100 calcium binding protein B Homo sapiens 103-106 8626429-6 1996 A functional proline-rich motif and the tyrosine phosphorylation of Nef were evidenced as likely participants in this interaction. Proline 13-20 S100 calcium binding protein B Homo sapiens 68-71 24051604-1 2013 The proline repeat motif (PxxP) of Nef is required for interaction with the SH3 domains of macrophage-specific Src kinase Hck. Proline 4-11 S100 calcium binding protein B Homo sapiens 35-38 26927806-7 2016 Coimmunoprecipitation and immunofluorescence analyses showed that ACOT8 Arg(45)-Phe(55) and Arg(86)-Pro(93) regions are involved in Nef association. Proline 100-103 S100 calcium binding protein B Homo sapiens 132-135 22651890-4 2012 We hypothesized that any Nef-SH3 domain interactions would be lost upon mutation of the prolines or arginine of PXXPXR. Proline 88-96 S100 calcium binding protein B Homo sapiens 25-28 22705789-3 2012 A ternary, cooperative interaction clamps the MHC-I CD into a narrow binding groove at the Nef-mu1 interface, which encompasses the cargo-recognition site of mu1 and the proline-rich strand of Nef. Proline 170-177 S100 calcium binding protein B Homo sapiens 91-94 22705789-3 2012 A ternary, cooperative interaction clamps the MHC-I CD into a narrow binding groove at the Nef-mu1 interface, which encompasses the cargo-recognition site of mu1 and the proline-rich strand of Nef. Proline 170-177 S100 calcium binding protein B Homo sapiens 193-196 22651890-6 2012 RESULTS: We found that mutations of either of the prolines or the arginine of PXXPXR are defective for Nef-Hck binding, Nef/activated PAK2 complex formation and enhancement of virion infectivity (EVI). Proline 50-58 S100 calcium binding protein B Homo sapiens 103-106 22651890-6 2012 RESULTS: We found that mutations of either of the prolines or the arginine of PXXPXR are defective for Nef-Hck binding, Nef/activated PAK2 complex formation and enhancement of virion infectivity (EVI). Proline 50-58 S100 calcium binding protein B Homo sapiens 120-123 22537596-3 2012 By studying the functionality of a series of nef alleles from clinical isolates, we identified a dysfunctional HIV group O Nef in which a highly conserved valine-glycine-phenylalanine (VGF) region, which links a preceding acidic cluster with the following proline-rich motif into an amphipathic surface was deleted. Proline 256-263 S100 calcium binding protein B Homo sapiens 45-48 22537596-3 2012 By studying the functionality of a series of nef alleles from clinical isolates, we identified a dysfunctional HIV group O Nef in which a highly conserved valine-glycine-phenylalanine (VGF) region, which links a preceding acidic cluster with the following proline-rich motif into an amphipathic surface was deleted. Proline 256-263 S100 calcium binding protein B Homo sapiens 123-126 22537596-11 2012 CONCLUSION: Based on these findings, we propose that this highly conserved three amino acid VGF motif together with the acidic cluster and the proline-rich motif form a previously unrecognized amphipathic surface on Nef. Proline 143-150 S100 calcium binding protein B Homo sapiens 216-219 22407921-8 2012 The myristoylation and proline-rich motif of Nef were responsible for the observed signaling activation. Proline 23-30 S100 calcium binding protein B Homo sapiens 45-48 18799583-7 2008 Nef-induced PD-1 upregulation requires its proline-rich motif and the activation of the downstream kinase p38. Proline 43-50 S100 calcium binding protein B Homo sapiens 0-3 21093412-2 2010 Some of these Nef activities are mediated by the well-conserved proline-rich region of Nef, and this region is highly targeted by cytotoxic T lymphocytes (CTLs). Proline 64-71 S100 calcium binding protein B Homo sapiens 14-17 21093412-2 2010 Some of these Nef activities are mediated by the well-conserved proline-rich region of Nef, and this region is highly targeted by cytotoxic T lymphocytes (CTLs). Proline 64-71 S100 calcium binding protein B Homo sapiens 87-90 21093412-4 2010 The analysis of autologous nef sequences isolated from a cohort of total 235 subjects in Japan revealed that the subjects showing amino acid variations, such as Arg75Thr and Tyr85Phe, located within the proline-rich region were significantly over-represented by those having HLA-B*3501. Proline 203-210 S100 calcium binding protein B Homo sapiens 27-30 18178851-3 2008 By genetic and functional studies, we found that Arg75Thr and Tyr85Phe mutations, located in a well-conserved proline-rich region in Nef, were differently associated with escape from CTL responses specific for two overlapping HLA-B35-restricted epitopes. Proline 110-117 S100 calcium binding protein B Homo sapiens 133-136 18707241-7 2008 We report that disruption of the proline-rich region of Nef inhibits T-cell migration to SDF-1 alpha. Proline 33-40 S100 calcium binding protein B Homo sapiens 56-59 10388555-7 1999 Data from these studies indicated that induction of AP-1 by Nef is likely to be mediated through the MAPK (ERK1 and 2) signaling pathway and requires the proline-rich PxxP motif of Nef, suggesting the involvement of upstream protein kinases belonging to the Src family. Proline 154-161 S100 calcium binding protein B Homo sapiens 60-63 16043695-5 2005 This activity requires a Src-kinase-binding proline-rich domain of Nef and a conserved tyrosine-based motif in the cytoplasmic tail of HFE. Proline 44-51 S100 calcium binding protein B Homo sapiens 67-70 10660579-9 2000 The herein described mechanism of SH3 selection by Nef via a "pocket" proximal to the canonical proline-rich motif may be a common feature for SH3 recognition by their natural ligands. Proline 96-103 S100 calcium binding protein B Homo sapiens 51-54 15976924-1 2005 The Nef protein of human immunodeficiency virus type 1 (HIV-1) is known to directly bind to the SH3 domain of human lymphocyte specific kinase (Lck) via a proline-rich region located in the amino terminal part of Nef. Proline 155-162 S100 calcium binding protein B Homo sapiens 213-216 11525746-4 2001 Here, we report that a natural variability in the proline-rich motif (R71T) profoundly modulated Nef-stimulated viral replication in primary T cells of immature dendritic cell/T cell cocultures. Proline 50-57 S100 calcium binding protein B Homo sapiens 97-100 10807905-4 2000 Interaction of Nef and hTE was abolished by point mutations in Nef at residues Asp(108), Leu(112), Phe(121), Pro(122), and Asp(123). Proline 109-112 S100 calcium binding protein B Homo sapiens 15-18 10807905-4 2000 Interaction of Nef and hTE was abolished by point mutations in Nef at residues Asp(108), Leu(112), Phe(121), Pro(122), and Asp(123). Proline 109-112 S100 calcium binding protein B Homo sapiens 63-66 10388555-7 1999 Data from these studies indicated that induction of AP-1 by Nef is likely to be mediated through the MAPK (ERK1 and 2) signaling pathway and requires the proline-rich PxxP motif of Nef, suggesting the involvement of upstream protein kinases belonging to the Src family. Proline 154-161 S100 calcium binding protein B Homo sapiens 181-184 9971776-0 1999 Nef-induced CD4 and major histocompatibility complex class I (MHC-I) down-regulation are governed by distinct determinants: N-terminal alpha helix and proline repeat of Nef selectively regulate MHC-I trafficking. Proline 151-158 S100 calcium binding protein B Homo sapiens 169-172 9971776-0 1999 Nef-induced CD4 and major histocompatibility complex class I (MHC-I) down-regulation are governed by distinct determinants: N-terminal alpha helix and proline repeat of Nef selectively regulate MHC-I trafficking. Proline 151-158 S100 calcium binding protein B Homo sapiens 0-3 9971776-8 1999 Although both the N-terminal alpha-helix and the proline-rich region of Nef have been implicated in recruiting Src family protein kinases, the inhibitor herbimycin A did not block MHC-I down-regulation, suggesting that the latter process is not mediated through an activation of this family of tyrosine kinases. Proline 49-56 S100 calcium binding protein B Homo sapiens 72-75 9705913-4 1998 Indeed, Nef contains a proline-rich motif implicated in the binding to the Src-like tyrosine kinase Hck and also to a Ser/Thr kinase of molecular weight 62 kDa. Proline 23-30 S100 calcium binding protein B Homo sapiens 8-11 9705913-8 1998 Both the proline motif and phosphorylation of Nef on tyrosine residue were proposed to account for these interactions. Proline 9-16 S100 calcium binding protein B Homo sapiens 46-49