1aws: Difference between revisions

Revision as of 17:45, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1aws.png

Template:STRUCTURE 1aws

SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)

Template:ABSTRACT PUBMED 9385632

About this StructureAbout this Structure

1AWS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein., Vajdos FF, Yoo S, Houseweart M, Sundquist WI, Hill CP, Protein Sci. 1997 Nov;6(11):2297-307. PMID:9385632

Page seeded by OCA on Mon Jun 30 17:45:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)'''
+===SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)===
-==Overview==
+<!--
-The cellular protein, cyclophilin A (CypA), is incorporated into the virion of the type 1 human immunodeficiency virus (HIV-1) via a direct interaction with the capsid domain of the viral Gag polyprotein. 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. In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. We also report the crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9385632}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9385632 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9385632}}
 ==About this Structure==
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 [[Category: Hiv-1 capsid]]
 [[Category: Pseudo-symmetry]]
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