Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein.

@article{Gamble1997StructureOT,
  title={Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein.},
  author={T. R. Gamble and Sanghee Yoo and Felix F. Vajdos and Uta K. von Schwedler and David K. Worthylake and H W Wang and John P. McCutcheon and Wesley I. Sundquist and Christopher P. Hill},
  journal={Science},
  year={1997},
  volume={278 5339},
  pages={
          849-53
        }
}
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… 

Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution.

CA146-231 and CA146-p2 dimerize with the full affinity of the intact capsid protein, and their structures therefore reveal the essential dimer interface of the HIV-1 capsid.

Domain-swapped dimerization of the HIV-1 capsid C-terminal domain

The observations suggest that swapping of the MHR segments of adjacent Gag molecules may be a critical intermediate in retroviral assembly, and an x-ray structure of a distinct domain-swapped variant of the HIV-1 CA-CTD dimer stabilized by a single amino acid deletion is described.

Flexibility in HIV-1 assembly subunits: solution structure of the monomeric C-terminal domain of the capsid protein.

The three-dimensional structure in aqueous solution of the monomeric mutant of CAC is solved and it is found that the structure is similar to that of the subunits in the dimeric, nonmutated CAC, except the segment corresponding to the second helix, which is highly dynamic.

A triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interface.

A novel triclinic structure of the HIV-1CA CTD at 1.6 Å resolution with two canonical dimers of CA CTD in the asymmetric unit is described, indicating the first structural indication that these MHR residues participate in the putative CTD-CTD interactions.

Structure and dynamics of full-length HIV-1 capsid protein in solution.

The structure and dynamics of full-length capsid protein in solution, comprising a mixture of monomeric and dimeric forms in dynamic equilibrium, are studied using ensemble simulated annealing driven by experimental NMR residual dipolar couplings and X-ray scattering data.

Implications for viral capsid assembly from crystal structures of HIV-1 Gag(1-278) and CA(N)(133-278).

Crystal structures of the mature CA N-terminal domain and a MA-CA(N) fusion are reported, which argue against the proposal that CypA binding is coupled with beta-hairpin formation and support an earlier surface plasmon resonance study.

Mutational Analysis and Allosteric Effects in the HIV-1 Capsid Protein Carboxyl-Terminal Dimerization Domain

Detailed structural analysis shows that three mutants display much more flexible local structures and weaker CA−CA association than the wild-type, primarily due to the loss of interactions with their neighboring residues, which indicates hydrophobic interactions, side chain packing, and hydrogen bonds are the major, dominant driving forces in stabilizing the CA interface.

Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein

Comparison of the immature and mature CAN structures reveals that β-hairpin formation induces a ∼2 Å displacement of helix 6 and a concomitant displacement of the cyclophylin-A (CypA)-binding loop, suggesting a possible allosteric mechanism for CypA-mediated destabilization of the capsid particle during infectivity.

Proline residues in the HIV-1 NH2-terminal capsid domain: structure determinants for proper core assembly and subsequent steps of early replication.

Results suggest that proline residues in the NH(2)-terminal capsid domain represent critical structure determinants for proper formation of functional virion cores and subsequent stages of early replication.

Structural mobility of the monomeric C‐terminal domain of the HIV‐1 capsid protein

A comprehensive examination of the CACW40A internal dynamics suggests a role for internal motions in the monomer–monomer interactions and flexibility of the polypeptide chain is likely to contribute to the ability of the protein to adopt different conformational states, depending on the biological environment.
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