Abstract:
:To investigate a conformational change accompanying peptide binding to class II MHC proteins, we probed the structure of a soluble version of the human class II MHC protein HLA-DR1 in empty and peptide-loaded forms. Peptide binding induced a large decrease in the effective radius of the protein as determined by gel filtration, dynamic light scattering, and analytical ultracentrifugation. It caused a substantial increase in the cooperativity of thermal denaturation and induced alterations in MHC polypeptide backbone structure as determined by circular dichroism. These changes suggest a condensation of the protein around the bound peptide. An antibody specific for beta58-69 preferentially bound the empty protein, indicating that the peptide-induced conformational change involves the beta-subunit helical region. The conformational change may have important implications for the mechanisms of intracellular antigen presentation pathways.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Zarutskie JA,Sato AK,Rushe MM,Chan IC,Lomakin A,Benedek GB,Stern LJdoi
10.1021/bi983048msubject
Has Abstractpub_date
1999-05-04 00:00:00pages
5878-87issue
18eissn
0006-2960issn
1520-4995pii
bi983048mjournal_volume
38pub_type
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