Structure and assembly of immature HIV Export

@article{citeulike:5120144, abstract = {10.1073/pnas.0903535106 The major structural components of HIV are synthesized as a 55-kDa polyprotein, Gag. Particle formation is driven by the self-assembly of Gag into a curved hexameric lattice, the structure of which is poorly understood. We used cryoelectron tomography and contrast-transfer-function corrected subtomogram averaging to study the structure of the assembled immature Gag lattice to ≈17-\r{A} resolution. Gag is arranged in the immature virus as a single, continuous, but incomplete hexameric lattice whose curvature is mediated without a requirement for pentameric defects. The resolution of the structure allows positioning of individual protein domains. High-resolution crystal structures were fitted into the reconstruction to locate protein–protein interfaces involved in Gag assembly, and to identify the structural transformations associated with virus maturation. The results of this study suggest a concept for the formation of nonsymmetrical enveloped viruses of variable sizes.}, author = {Briggs, J. A. G. and Riches, J. D. and Glass, B. and Bartonova, V. and Zanetti, G. and Kr\"{a}usslich, H. G.}, citeulike-article-id = {5120144}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0903535106}, citeulike-linkout-1 = {http://www.pnas.org/content/106/27/11090.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/106/27/11090.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19549863}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19549863}, day = {7}, doi = {10.1073/pnas.0903535106}, journal = {Proceedings of the National Academy of Sciences}, keywords = {assembly, hiv, structure}, month = {July}, number = {27}, pages = {11090--11095}, posted-at = {2009-07-14 12:20:39}, priority = {2}, title = {Structure and assembly of immature HIV}, url = {http://dx.doi.org/10.1073/pnas.0903535106}, volume = {106}, year = {2009} }

TY - JOUR ID - citeulike:5120144 L3 - citeulike-article-id:5120144 N2 - 10.1073/pnas.0903535106 The major structural components of HIV are synthesized as a 55-kDa polyprotein, Gag. Particle formation is driven by the self-assembly of Gag into a curved hexameric lattice, the structure of which is poorly understood. We used cryoelectron tomography and contrast-transfer-function corrected subtomogram averaging to study the structure of the assembled immature Gag lattice to ≈17-Å resolution. Gag is arranged in the immature virus as a single, continuous, but incomplete hexameric lattice whose curvature is mediated without a requirement for pentameric defects. The resolution of the structure allows positioning of individual protein domains. High-resolution crystal structures were fitted into the reconstruction to locate protein–protein interfaces involved in Gag assembly, and to identify the structural transformations associated with virus maturation. The results of this study suggest a concept for the formation of nonsymmetrical enveloped viruses of variable sizes. IS - 27 JF - Proceedings of the National Academy of Sciences EP - 11095 TI - Structure and assembly of immature HIV VL - 106 SP - 11090 KW - assembly KW - hiv KW - structure AU - Briggs, JAG AU - Riches, JD AU - Glass, B AU - Bartonova, V AU - Zanetti, G AU - Kräusslich, HG PY - 2009/07/07/ UR - http://dx.doi.org/10.1073/pnas.0903535106 ER -