1ak4: Difference between revisions

Revision as of 17:01, 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:1ak4.png

Template:STRUCTURE 1ak4

HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSIDHUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID

Template:ABSTRACT PUBMED 8980234

About this StructureAbout this Structure

1AK4 is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid., Gamble TR, Vajdos FF, Yoo S, Worthylake DK, Houseweart M, Sundquist WI, Hill CP, Cell. 1996 Dec 27;87(7):1285-94. PMID:8980234

Page seeded by OCA on Mon Jun 30 17:01:01 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ak4.jpg|left|200px]]
+{{Seed}}
+[[Image:1ak4.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ak4|  PDB=1ak4  |  SCENE=  }}
-'''HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID'''
+===HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID===
-==Overview==
+<!--
-The HIV-1 capsid protein forms the conical core structure at the center of the mature virion. Capsid also binds the human peptidyl prolyl isomerase, cyclophilin A, thereby packaging the enzyme into the virion. Cyclophilin A subsequently performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection. We report the 2.36 A crystal structure of the N-terminal domain of HIV-1 capsid (residues 1-151) in complex with human cyclophilin A. A single exposed capsid loop (residues 85-93) binds in the enzyme's active site, and Pro-90 adopts an unprecedented trans conformation. The structure suggests how cyclophilin A can act as a sequence-specific binding protein and a nonspecific prolyl isomerase. In the crystal lattice, capsid molecules assemble into continuous planar strips. Side by side association of these strips may allow capsid to form the surface of the viral core. Cyclophilin A could then function by weakening the association between capsid strips, thereby promoting disassembly of the viral core.
+The line below this paragraph, {{ABSTRACT_PUBMED_8980234}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8980234 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8980234}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Hiv-1]]
 [[Category: Isomerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:22:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:01:01 2008''