1a8o

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1a8o, resolution 1.70Å

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HIV CAPSID C-TERMINAL DOMAIN

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

1A8O is a Single protein structure of sequence from Human immunodeficiency virus 1. This structure superseeds the now removed PDB entry 1AM3. 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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