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1awr

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1awr, resolution 1.58Å ()
Gene: CYCLOPHILIN (Homo sapiens)
Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

CYPA COMPLEXED WITH HAGPIA

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1awr is a 12 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

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

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