TY - JOUR
T1 - Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
AU - Gamble, Theresa R.
AU - Yoo, Sanghee
AU - Vajdos, Felix F.
AU - Von Schwedler, Uta K.
AU - Worthylake, David K.
AU - Wang, Hui
AU - McCutcheon, John P.
AU - Sundquist, Wesley I.
AU - Hill, Christopher P.
PY - 1997/10/31
Y1 - 1997/10/31
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0030693391&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030693391&partnerID=8YFLogxK
U2 - 10.1126/science.278.5339.849
DO - 10.1126/science.278.5339.849
M3 - Article
C2 - 9346481
AN - SCOPUS:0030693391
SN - 0036-8075
VL - 278
SP - 849
EP - 853
JO - Science
JF - Science
IS - 5339
ER -