PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17098251-6 2007 We have now explored the binding of inositol hexakisphosphate (IP6) to Gag and its effects upon the interactions between Gag protein molecules in solution. Phytic Acid 36-61 Pr55(Gag) Human immunodeficiency virus 1 71-74 17098251-6 2007 We have now explored the binding of inositol hexakisphosphate (IP6) to Gag and its effects upon the interactions between Gag protein molecules in solution. Phytic Acid 36-61 Pr55(Gag) Human immunodeficiency virus 1 121-124 17098251-6 2007 We have now explored the binding of inositol hexakisphosphate (IP6) to Gag and its effects upon the interactions between Gag protein molecules in solution. Phytic Acid 63-66 Pr55(Gag) Human immunodeficiency virus 1 71-74 17098251-6 2007 We have now explored the binding of inositol hexakisphosphate (IP6) to Gag and its effects upon the interactions between Gag protein molecules in solution. Phytic Acid 63-66 Pr55(Gag) Human immunodeficiency virus 1 121-124 17098251-9 2007 In contrast, when IP6 is added, Gag is in monomer-trimer rather than monomer-dimer equilibrium. Phytic Acid 18-21 Pr55(Gag) Human immunodeficiency virus 1 32-35 17098251-10 2007 The Gag protein with a mutation at the dimer interface also remains almost exclusively monomeric in IP6; thus the "dimer interface" is essential for the trimeric interaction in IP6. Phytic Acid 100-103 Pr55(Gag) Human immunodeficiency virus 1 4-7 17098251-10 2007 The Gag protein with a mutation at the dimer interface also remains almost exclusively monomeric in IP6; thus the "dimer interface" is essential for the trimeric interaction in IP6. Phytic Acid 177-180 Pr55(Gag) Human immunodeficiency virus 1 4-7 17098251-12 2007 The participation of both ends of Gag in IP6 interaction suggests that Gag is folded over in solution, with its ends near each other in three-dimensional space; direct support for this conclusion is provided in a companion manuscript. Phytic Acid 41-44 Pr55(Gag) Human immunodeficiency virus 1 34-37 17098251-12 2007 The participation of both ends of Gag in IP6 interaction suggests that Gag is folded over in solution, with its ends near each other in three-dimensional space; direct support for this conclusion is provided in a companion manuscript. Phytic Acid 41-44 Pr55(Gag) Human immunodeficiency virus 1 71-74 34578434-2 2021 However, the molecular details underlying this effect have been determined only recently, with the identification of the IP6 binding site in the immature Gag lattice. Phytic Acid 121-124 Pr55(Gag) Human immunodeficiency virus 1 154-157 32727872-3 2020 IP6 participates in the proper assembly of Gag into immature hexameric lattices and is incorporated into HIV-1 particles. Phytic Acid 0-3 Pr55(Gag) Human immunodeficiency virus 1 43-46 34454514-2 2021 Virion assembly and maturation are facilitated by the cellular polyanion inositol hexaphosphate (IP6), which is proposed to stabilize both the immature Gag lattice and the mature capsid lattice by binding to rings of primary amines at the center of Gag or capsid protein (CA) hexamers. Phytic Acid 97-100 Pr55(Gag) Human immunodeficiency virus 1 152-155 34454514-2 2021 Virion assembly and maturation are facilitated by the cellular polyanion inositol hexaphosphate (IP6), which is proposed to stabilize both the immature Gag lattice and the mature capsid lattice by binding to rings of primary amines at the center of Gag or capsid protein (CA) hexamers. Phytic Acid 97-100 Pr55(Gag) Human immunodeficiency virus 1 249-252 34454514-5 2021 RESULTS: We found a mutation, a threonine to isoleucine substitution at position 371 (T371I) in Gag, that restored replication competence to an IP6-binding-deficient HIV-1 mutant. Phytic Acid 144-147 Pr55(Gag) Human immunodeficiency virus 1 96-99 34454514-9 2021 CONCLUSIONS: Overall these results suggest that IP6-Gag and Gag-Gag contacts are finely tuned to generate a Gag lattice of optimal stability, and that under certain conditions BVM can rescue IP6 deficiency. Phytic Acid 48-51 Pr55(Gag) Human immunodeficiency virus 1 52-55 34454514-9 2021 CONCLUSIONS: Overall these results suggest that IP6-Gag and Gag-Gag contacts are finely tuned to generate a Gag lattice of optimal stability, and that under certain conditions BVM can rescue IP6 deficiency. Phytic Acid 48-51 Pr55(Gag) Human immunodeficiency virus 1 108-111 34349176-2 2021 It has been known that the binding of IP6, an abundant endogenous cyclitol molecule at the MA domain, has been linked to the oligomerization of Pr55Gag. Phytic Acid 38-41 Pr55(Gag) Human immunodeficiency virus 1 144-151 34349176-6 2021 Our data provide novel insights about the multilayered HIV-1 virion assembly process that involves the interplay of IP6 with PIP2, a phosphoinositide essential for the binding of Pr55Gag to membrane. Phytic Acid 116-119 Pr55(Gag) Human immunodeficiency virus 1 179-186 33476323-4 2021 Moreover, HIV-1 substitutions bearing Gag/CA mutations ablating IP6 binding are noninfectious with destabilized viral cores. Phytic Acid 64-67 Pr55(Gag) Human immunodeficiency virus 1 38-41 31437199-7 2019 Sequence analysis shows high conservation within the newly-found intra-Gag MA/CActd binding site, as well as its spatial proximity to other well known elements of Gag -such as CActd"s SP1 helix region, its inositol hexaphosphate (IP6) binding site and major homology region (MHR), as well as the MA trimerization site. Phytic Acid 230-233 Pr55(Gag) Human immunodeficiency virus 1 71-74 31437199-7 2019 Sequence analysis shows high conservation within the newly-found intra-Gag MA/CActd binding site, as well as its spatial proximity to other well known elements of Gag -such as CActd"s SP1 helix region, its inositol hexaphosphate (IP6) binding site and major homology region (MHR), as well as the MA trimerization site. Phytic Acid 230-233 Pr55(Gag) Human immunodeficiency virus 1 163-166 30987231-0 2019 Serial Femtosecond X-Ray Diffraction of HIV-1 Gag MA-IP6 Microcrystals at Ambient Temperature. Phytic Acid 53-56 Pr55(Gag) Human immunodeficiency virus 1 46-49 30987231-7 2019 Two different microcrystal forms of the MA-IP6 complex both diffracted to beyond 3.5 A resolution, demonstrating the feasibility of using SFX to study the complexes of MA domain of HIV-1 Gag polyprotein with IP6 at near-physiological temperatures. Phytic Acid 43-46 Pr55(Gag) Human immunodeficiency virus 1 187-190 30987231-7 2019 Two different microcrystal forms of the MA-IP6 complex both diffracted to beyond 3.5 A resolution, demonstrating the feasibility of using SFX to study the complexes of MA domain of HIV-1 Gag polyprotein with IP6 at near-physiological temperatures. Phytic Acid 208-211 Pr55(Gag) Human immunodeficiency virus 1 187-190 30987231-8 2019 Further optimization of the experimental and data analysis procedures will lead to better understanding of the MA domain of HIV-1 Gag and IP6 interaction at high resolution and will provide basis for optimization of the lead compounds for efficient inhibition of the Gag protein recruitment to the plasma membrane prior to virion formation. Phytic Acid 138-141 Pr55(Gag) Human immunodeficiency virus 1 267-270 21045546-11 2010 In one system, binding of nucleic acid by the matrix domain of Gag retarded the Gag-induced annealing of two RNAs; this effect could be ameliorated by the competitive binding of inositol hexakisphosphate to the matrix domain. Phytic Acid 178-203 Pr55(Gag) Human immunodeficiency virus 1 63-66 24403576-6 2014 However, with the addition of inositol hexakisphosphate, Gag adopts a linear conformation and assembles into full-sized ~100-to-150-nm-diameter VLPs. Phytic Acid 30-55 Pr55(Gag) Human immunodeficiency virus 1 57-60 30069050-5 2018 Here, using a combination of structural and functional analyses, we show that inositol hexakisphosphate (InsP6, also known as IP6) facilitates the formation of the six-helix bundle and assembly of the immature HIV-1 Gag lattice. Phytic Acid 78-103 Pr55(Gag) Human immunodeficiency virus 1 216-219 30069050-5 2018 Here, using a combination of structural and functional analyses, we show that inositol hexakisphosphate (InsP6, also known as IP6) facilitates the formation of the six-helix bundle and assembly of the immature HIV-1 Gag lattice. Phytic Acid 126-129 Pr55(Gag) Human immunodeficiency virus 1 216-219 30069050-6 2018 IP6 makes ionic contacts with two rings of lysine residues at the centre of the Gag hexamer. Phytic Acid 0-3 Pr55(Gag) Human immunodeficiency virus 1 80-83 21045546-11 2010 In one system, binding of nucleic acid by the matrix domain of Gag retarded the Gag-induced annealing of two RNAs; this effect could be ameliorated by the competitive binding of inositol hexakisphosphate to the matrix domain. Phytic Acid 178-203 Pr55(Gag) Human immunodeficiency virus 1 80-83 19073719-10 2009 However, addition of both IPs and nucleic acid leads to correct assembly of all three proteins; the "dimerizing" Gag-Zipper protein also assembles correctly if inositol hexakisphosphate is supplemented with other polyanions. Phytic Acid 160-185 Pr55(Gag) Human immunodeficiency virus 1 113-116