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1sea
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| - | + | ==RESIDUES DEFINING VBETA SPECIFICITY IN STAPHYLOCOCCAL ENTEROTOXINS== | |
| + | <StructureSection load='1sea' size='340' side='right' caption='[[1sea]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SEA FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sea FirstGlance], [http://www.ebi.ac.uk/pdbsum/1sea PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The three-dimensional structure of staphylococcal enterotoxin C2 has been determined at 2.7 A resolution by x-ray diffraction, while the structures of enterotoxins A and E have been modelled based on their sequence homology to other staphylococcal enterotoxins. The T-cell receptor-binding sites of staphylococcal enterotoxin (SE) B and SEC2 are compared and the stereochemical interactions likely to be responsible for their differing V beta specificities are identified. A similar comparison is made between SEA and SEE. | ||
| - | + | Residues defining V beta specificity in staphylococcal enterotoxins.,Swaminathan S, Furey W, Pletcher J, Sax M Nat Struct Biol. 1995 Aug;2(8):680-6. PMID:7552730<ref>PMID:7552730</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | == References == |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | < | + | |
[[Category: Sax, M]] | [[Category: Sax, M]] | ||
[[Category: Swaminathan, S]] | [[Category: Swaminathan, S]] | ||
Revision as of 20:22, 28 September 2014
RESIDUES DEFINING VBETA SPECIFICITY IN STAPHYLOCOCCAL ENTEROTOXINS
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