1see

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Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

RESIDUES DEFINING VBETA SPECIFICITY IN STAPHYLOCOCCAL ENTEROTOXINS

Structural highlights

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Resources:	FirstGlance, PDBsum, ProSAT

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

↑ Swaminathan S, Furey W, Pletcher J, Sax M. Residues defining V beta specificity in staphylococcal enterotoxins. Nat Struct Biol. 1995 Aug;2(8):680-6. PMID:7552730

1 Structural highlights
2 Publication Abstract from PubMed
3 References

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PDB ID 1see

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Categories: Theoretical Model | Large Structures | Sax, M | Swaminathan, S

1see

From Proteopedia

RESIDUES DEFINING VBETA SPECIFICITY IN STAPHYLOCOCCAL ENTEROTOXINS

Structural highlights

Publication Abstract from PubMed

References

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