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Superantigen architecture: Functional decoration on a conserved scaffold

Abstract
A defining and consistent feature of the bacterial superantigens from Staphylococcus aureus and Streptococcus pyogenes is their strongly conserved three-dimensional structure. Structural studies to date show that the array of more than 280 amino acid sequences known for superantigens (SAgs) and staphylococcal superantigen-like (SSL) proteins all have the same fold-a structure in which the same three-dimensional arrangement of α-helices and β-sheets is traced by each amino acid sequence, with the same topology (for recent reviews, see references 29 and 43). A typical SAg structure comprises two domains-an N-terminal β -barrel domain called an OB-fold (4, 25) and a C-terminal β-grasp domain in which a long α-helix packs on to a mixed parallel and antiparallel β-sheet. These two domains are traversed by an α-helix that lies at the N terminus of the protein and packs against the β-grasp domain, thus linking the N- and C-terminal domains.
Type
Chapter in Book
Type of thesis
Series
Citation
Arcus, V.L. & Baker, E.N. (2007). Superantigen architecture: Functional decoration on a conserved scaffold. In M. Kotb & J.D. Fraser (Eds.), Superantigens: Molecular Basis for Their Role in Human Diseases (pp. 93-102). Washington, D.C., United States of America: ASM Press.
Date
2007
Publisher
ASM Press
Degree
Supervisors
Rights
This chapter has been published in the book: Superantigens: Molecular Basis for Their Role in Human Diseases. © 2007 ASM Press. Used with permission.