3j0f: Difference between revisions
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[[ | ==Sindbis virion== | ||
<StructureSection load='3j0f' size='340' side='right' caption='[[3j0f]], [[Resolution|resolution]] 7.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3j0f]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Sindbis_virus Sindbis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J0F FirstGlance]. <br> | |||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Togavirin Togavirin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.90 3.4.21.90] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j0f RCSB], [http://www.ebi.ac.uk/pdbsum/3j0f PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A three-dimensional reconstruction of Sindbis virus at 7.0 A resolution presented here provides a detailed view of the virion structure and includes structural evidence for key interactions that occur between the capsid protein (CP) and transmembrane (TM) glycoproteins E1 and E2. Based on crystal structures of component proteins and homology modeling, we constructed a nearly complete, pseudo-atomic model of the virus. Notably, this includes identification of the 33-residue cytoplasmic domain of E2 (cdE2), which follows a path from the E2 TM helix to the CP where it enters and exits the CP hydrophobic pocket and then folds back to contact the viral membrane. Modeling analysis identified three major contact regions between cdE2 and CP, and the roles of specific residues were probed by molecular genetics. This identified R393 and E395 of cdE2 and Y162 and K252 of CP as critical for virus assembly. The N-termini of the CPs form a contiguous network that interconnects 12 pentameric and 30 hexameric CP capsomers. A single glycoprotein spike cross-links three neighboring CP capsomers as might occur during initiation of virus budding. | |||
Molecular Links between the E2 Envelope Glycoprotein and Nucleocapsid Core in Sindbis Virus.,Tang J, Jose J, Chipman P, Zhang W, Kuhn RJ, Baker TS J Mol Biol. 2011 Oct 4. PMID:22001018<ref>PMID:22001018</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Virus coat protein|Virus coat protein]] | *[[Virus coat protein|Virus coat protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Sindbis virus]] | [[Category: Sindbis virus]] | ||
[[Category: Togavirin]] | [[Category: Togavirin]] | ||
[[Category: Baker, T S | [[Category: Baker, T S]] | ||
[[Category: Chipman, P | [[Category: Chipman, P]] | ||
[[Category: Jose, J | [[Category: Jose, J]] | ||
[[Category: Kuhn, R J | [[Category: Kuhn, R J]] | ||
[[Category: Tang, J | [[Category: Tang, J]] | ||
[[Category: Zhang, W | [[Category: Zhang, W]] | ||
[[Category: Alphavirus]] | [[Category: Alphavirus]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
[[Category: Virus]] | [[Category: Virus]] | ||
[[Category: Virus assembly]] | [[Category: Virus assembly]] | ||
Revision as of 12:28, 8 December 2014
Sindbis virionSindbis virion
Structural highlights
Publication Abstract from PubMedA three-dimensional reconstruction of Sindbis virus at 7.0 A resolution presented here provides a detailed view of the virion structure and includes structural evidence for key interactions that occur between the capsid protein (CP) and transmembrane (TM) glycoproteins E1 and E2. Based on crystal structures of component proteins and homology modeling, we constructed a nearly complete, pseudo-atomic model of the virus. Notably, this includes identification of the 33-residue cytoplasmic domain of E2 (cdE2), which follows a path from the E2 TM helix to the CP where it enters and exits the CP hydrophobic pocket and then folds back to contact the viral membrane. Modeling analysis identified three major contact regions between cdE2 and CP, and the roles of specific residues were probed by molecular genetics. This identified R393 and E395 of cdE2 and Y162 and K252 of CP as critical for virus assembly. The N-termini of the CPs form a contiguous network that interconnects 12 pentameric and 30 hexameric CP capsomers. A single glycoprotein spike cross-links three neighboring CP capsomers as might occur during initiation of virus budding. Molecular Links between the E2 Envelope Glycoprotein and Nucleocapsid Core in Sindbis Virus.,Tang J, Jose J, Chipman P, Zhang W, Kuhn RJ, Baker TS J Mol Biol. 2011 Oct 4. PMID:22001018[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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