PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15229879-9	2004	The results show that CA(N) residues His87-Ala-Gly-Pro-Ile-Ala92 form the majority of the interactions with CypA residues.	Glycine	47-50	peptidylprolyl isomerase A	Homo sapiens	108-112	
9385632-2	1997	We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex.	Glycine	50-53	peptidylprolyl isomerase A	Homo sapiens	105-118	
15147195-1	2004	The prolyl isomerase cyclophilin A (CypA) is required for efficient HIV-1 replication and is incorporated into virions through a binding interaction at the Gly-Pro(222) bond located within the capsid domain of the HIV-1 Gag precursor polyprotein (Pr(gag)).	Glycine	156-159	peptidylprolyl isomerase A	Homo sapiens	36-40	
15147195-3	2004	To address the proposal that CypA interacts with Gly-Pro sequences in the C-terminal domain of a mature capsid, the interaction between CypA and the natively folded, full-length capsid protein (CA(FL)) has been investigated here using nuclear magnetic resonance spectroscopy.	Glycine	49-52	peptidylprolyl isomerase A	Homo sapiens	29-33	
11929983-4	2002	We show here, using NMR exchange spectroscopy, that CypA does not only bind to CA(N) but also catalyzes efficiently the cis/trans isomerization of the Gly-89-Pro-90 peptide bond.	Glycine	151-154	peptidylprolyl isomerase A	Homo sapiens	52-56	
10026140-2	1999	CyPA binds to the previously identified Gly-Pro90 site of the capsid protein p24, but its role remained unclear.	Glycine	40-43	peptidylprolyl isomerase A	Homo sapiens	0-4	
10026140-5	1999	Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins.	Glycine	166-169	peptidylprolyl isomerase A	Homo sapiens	104-108	
10026140-5	1999	Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins.	Glycine	166-169	peptidylprolyl isomerase A	Homo sapiens	327-339	
10026140-6	1999	Between CyPA and an immature (unprocessed) form of p24, a Kd of approximately 8 microM was measured, which corresponded with the Kd of the best of the Gly-Pro90 peptides, indicating an association via this site.	Glycine	151-154	peptidylprolyl isomerase A	Homo sapiens	8-12	
9385632-5	1997	Comparison with the recently determined structures of CypA in complexes with larger fragments of the HIV-1 capsid protein demonstrates that CypA recognition of these hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences.	Glycine	232-235	peptidylprolyl isomerase A	Homo sapiens	140-144	
9385632-2	1997	We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex.	Glycine	50-53	peptidylprolyl isomerase A	Homo sapiens	178-182	
24991000-3	2014	Inspection of the CA sequences of lentiviruses reveals that several species of simian immunodeficiency viruses (SIVs) have lost the glycine-proline motif in the helix 4-5 loop important for CypA binding; instead, the helix 4-5 loop in these SIVs exhibits an increase in the number of glutamine residues.	Glycine	132-139	peptidylprolyl isomerase A	Homo sapiens	190-194	
9032343-2	1997	Elucidation of the biochemical role of CyPA would be aided by a detailed analysis of the genetic requirements for the formation of the Gag-CyPA complex; previous experiments have demonstrated the requirement for a critical proline and the immediately preceding glycine, located within the capsid domain of Gag, but nothing is known about the necessary CyPA residues.	Glycine	261-268	peptidylprolyl isomerase A	Homo sapiens	39-43