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Evidence for the alpha-helicity of class II MHC molecular binding sites for the superantigen, staphylococcal enterotoxin A.

Abstract：

:Circular dichroism (CD) spectra of class II MHC peptides revealed the alpha-helical conformation of superantigen-binding peptides I-A beta b(60-90), I-A beta b(65-85), and I-A alpha b(51-80), but not the nonbinding peptide I-A beta b(80-100). These CD spectra provide biophysical evidence for the alpha-helicity of class II MHC molecular binding sites for the superantigen, staphylococcal enterotoxin A (SEA). Alanine-substituted analogs of the SEA binding-site peptide, I-A beta b(65-85), were used to implicate beta-chain residues 72 and 80 in class II MHC-SEA binding. The data support SEA binding away from the class II antigen binding cleft along the faces of the alpha-helices.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Russell JK,Jarpe MA,Johnson HM

doi

10.1016/0006-291x(92)91833-c

subject

Has Abstract

pub_date

1992-02-14 00:00:00

pages

1016-24

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)91833-C

journal_volume

182

pub_type

杂志文章

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