1aws

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[[Image:1aws.jpg|left|200px]]
[[Image:1aws.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1aws |SIZE=350|CAPTION= <scene name='initialview01'>1aws</scene>, resolution 2.55&Aring;
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The line below this paragraph, containing "STRUCTURE_1aws", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1aws| PDB=1aws | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aws OCA], [http://www.ebi.ac.uk/pdbsum/1aws PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aws RCSB]</span>
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}}
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'''SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)'''
'''SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Vajdos, F F.]]
[[Category: Vajdos, F F.]]
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[[Category: complex (isomerase/peptide)]]
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[[Category: Cyclophilin some]]
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[[Category: cyclophilin some]]
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[[Category: Hiv-1 capsid]]
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[[Category: hiv-1 capsid]]
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[[Category: Pseudo-symmetry]]
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[[Category: pseudo-symmetry]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:47:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:58 2008''
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Revision as of 07:47, 2 May 2008

Image:1aws.jpg

Template:STRUCTURE 1aws

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. 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 Page seeded by OCA on Fri May 2 10:47:19 2008

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