1fod: Difference between revisions
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<StructureSection load='1fod' size='340' side='right'caption='[[1fod]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1fod' size='340' side='right'caption='[[1fod]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fod]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1fod]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fmdv Fmdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOD FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fod OCA], [https://pdbe.org/1fod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fod RCSB], [https://www.ebi.ac.uk/pdbsum/1fod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fod ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Virus coat | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:12, 28 July 2021
STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUSSTRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUS
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAttachment of foot-and-mouth disease virus (FMDV) to its cellular receptor involves a long and highly antigenic loop containing the conserved sequence, Arg-Gly-Asp, a motif known to be a recognition element in many integrin-dependent cell adhesion processes. In our original crystal structure of FMDV the Arg-Gly-Asp-containing loop ('the loop'), located between beta-strands G and H of capsid protein VP1, was disordered and hence essentially invisible. We previously surmised that its disorder is enhanced by a disulphide bond linking the base of the loop (Cys 134) to Cys 130 of VP2 (ref. 8). We report here the crystal structure of the virus in which this disulphide is reduced. Reduced virus retains infectivity and serological experiments suggest that some of the loop's internal structure is conserved. But here its structure has become sufficiently ordered to allow us to describe an unambiguous conformation, which we relate to some key biological properties of the virus. Structure of a major immunogenic site on foot-and-mouth disease virus.,Logan D, Abu-Ghazaleh R, Blakemore W, Curry S, Jackson T, King A, Lea S, Lewis R, Newman J, Parry N, et al. Nature. 1993 Apr 8;362(6420):566-8. PMID:8385272[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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