1fod
From Proteopedia
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| - | [[Image:1fod.gif|left|200px]] | + | [[Image:1fod.gif|left|200px]] |
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| - | '''STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUS''' | + | {{Structure |
| + | |PDB= 1fod |SIZE=350|CAPTION= <scene name='initialview01'>1fod</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FOD is a [ | + | 1FOD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOD OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8385272 8385272] |
[[Category: Foot-and-mouth disease virus]] | [[Category: Foot-and-mouth disease virus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: virus]] | [[Category: virus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:48 2008'' |
Revision as of 09:11, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUS
Overview
Attachment 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.
About this Structure
1FOD is a Protein complex structure of sequences from Foot-and-mouth disease virus. Full crystallographic information is available from OCA.
Reference
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
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