1aws
From Proteopedia
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| - | [[Image:1aws. | + | [[Image:1aws.jpg|left|200px]]<br /><applet load="1aws" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1aws" size=" | + | |
caption="1aws, resolution 2.55Å" /> | caption="1aws, resolution 2.55Å" /> | ||
'''SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)'''<br /> | '''SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AWS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http:// | + | 1AWS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pseudo-symmetry]] | [[Category: pseudo-symmetry]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:30:03 2008'' |
Revision as of 13:30, 15 February 2008
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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.
About this Structure
1AWS is a Single protein structure of sequence from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
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
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