1aum
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(New page: 200px<br /> <applet load="1aum" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aum, resolution 3.0Å" /> '''HIV CAPSID C-TERMINA...)
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Revision as of 11:45, 8 November 2007
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HIV CAPSID C-TERMINAL DOMAIN (CAC146)
Overview
The carboxyl-terminal domain, residues 146 to 231, of the human, immunodeficiency virus-1 (HIV-1) capsid protein [CA(146-231)] is required, for capsid dimerization and viral assembly. This domain contains a stretch, of 20 residues, called the major homology region (MHR), which is conserved, across retroviruses and is essential for viral assembly, maturation, and, infectivity. The crystal structures of CA(146-231) and CA(151-231) reveal, that the globular domain is composed of four helices and an extended, amino-terminal strand. CA(146-231) dimerizes through parallel packing of, helix 2 across a dyad. The MHR is distinct from the dimer interface and, instead forms an intricate hydrogen-bonding network that interconnects, strand 1 and helices 1 and 2. Alignment of the CA(146-231) dimer with the, crystal structure of the capsid amino-terminal domain provides a model for, the intact protein and extends models for assembly of the central conical, core of HIV-1.
About this Structure
1AUM is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein., Gamble TR, Yoo S, Vajdos FF, von Schwedler UK, Worthylake DK, Wang H, McCutcheon JP, Sundquist WI, Hill CP, Science. 1997 Oct 31;278(5339):849-53. PMID:9346481
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