This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1aws

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1aws.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1aws.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1aws| PDB=1aws | SCENE= }}
{{STRUCTURE_1aws| PDB=1aws | SCENE= }}
-
'''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==
==About this Structure==
Line 27: Line 31:
[[Category: Hiv-1 capsid]]
[[Category: Hiv-1 capsid]]
[[Category: Pseudo-symmetry]]
[[Category: Pseudo-symmetry]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:47:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:45:34 2008''

Revision as of 14:45, 30 June 2008

Image:1aws.png

Template:STRUCTURE 1aws

SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)

Template:ABSTRACT PUBMED 9385632

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 Mon Jun 30 17:45:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aws"
Personal tools