Conformational changes of the flavivirus E glycoprotein. Export

@article{citeulike:4532804, abstract = {Dengue virus, a member of the Flaviviridae family, has a surface composed of 180 copies each of the envelope (E) glycoprotein and the membrane (M) protein. The crystal structure of an N-terminal fragment of E has been determined and compared with a previously described structure. The primary difference between these structures is a 10 degrees rotation about a hinge relating the fusion domain DII to domains DI and DIII. These two rigid body components were used for independent fitting of E into the cryo-electron microscopy maps of both immature and mature dengue viruses. The fitted E structures in these two particles showed a difference of 27 degrees between the two components. Comparison of the E structure in its postfusion state with that in the immature and mature virions shows a rotation approximately around the same hinge. Flexibility of E is apparently a functional requirement for assembly and infection of flaviviruses.}, author = {Zhang, Ying and Zhang, Wei and Ogata, Steven and Clements, David and Strauss, James H. and Baker, Timothy S. and Kuhn, Richard J. and Rossmann, Michael G.}, citeulike-article-id = {4532804}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.str.2004.06.019}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0969212604002722}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/15341726}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=15341726}, doi = {10.1016/j.str.2004.06.019}, issn = {0969-2126}, journal = {Structure (London, England : 1993)}, month = {September}, number = {9}, pages = {1607--1618}, posted-at = {2009-09-10 23:34:26}, priority = {2}, title = {Conformational changes of the flavivirus E glycoprotein.}, url = {http://dx.doi.org/10.1016/j.str.2004.06.019}, volume = {12}, year = {2004} }

TY - JOUR ID - citeulike:4532804 L3 - citeulike-article-id:4532804 N2 - Dengue virus, a member of the Flaviviridae family, has a surface composed of 180 copies each of the envelope (E) glycoprotein and the membrane (M) protein. The crystal structure of an N-terminal fragment of E has been determined and compared with a previously described structure. The primary difference between these structures is a 10 degrees rotation about a hinge relating the fusion domain DII to domains DI and DIII. These two rigid body components were used for independent fitting of E into the cryo-electron microscopy maps of both immature and mature dengue viruses. The fitted E structures in these two particles showed a difference of 27 degrees between the two components. Comparison of the E structure in its postfusion state with that in the immature and mature virions shows a rotation approximately around the same hinge. Flexibility of E is apparently a functional requirement for assembly and infection of flaviviruses. IS - 9 JF - Structure (London, England : 1993) SN - 0969-2126 EP - 1618 TI - Conformational changes of the flavivirus E glycoprotein. VL - 12 SP - 1607 AU - Zhang, Ying AU - Zhang, Wei AU - Ogata, Steven AU - Clements, David AU - Strauss, James AU - Baker, Timothy AU - Kuhn, Richard AU - Rossmann, Michael PY - 2004/09// UR - http://dx.doi.org/10.1016/j.str.2004.06.019 ER -