Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein.
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.
Gamble
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TR
Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.
Yoo
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S
Vajdos
F F
FF
von Schwedler
U K
UK
Worthylake
D K
DK
Wang
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H
McCutcheon
J P
JP
Sundquist
W I
WI
Hill
C P
CP
D000595:Amino Acid Sequence; D001665:Binding Sites; D002213:Capsid / Q000737:chemistry* / Q000235:genetics; D002460:Cell Line; D003001:Cloning, Molecular; D019976:Cloning, Organism; D018360:Crystallography, X-Ray; D019281:Dimerization; D015497:HIV-1 / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019696:Peptidylprolyl Isomerase / Q000737:chemistry; D011487:Protein Conformation; D014779:Virus Replication
D019696:Peptidylprolyl Isomerase