Crystal Structure of the HLA-DM–HLA-DR1 Complex Defines Mechanisms for Rapid Peptide Selection-Reference-Cited by-同舟云学术

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Crystal Structure of the HLA-DM–HLA-DR1 Complex Defines Mechanisms for Rapid Peptide Selection

Published:2012-12 Issue:7 Volume:151 Page:1557-1568
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Pos Wouter,Sethi Dhruv K.,Call Melissa J.,Schulze Monika-Sarah E.D.,Anders Anne-Kathrin,Pyrdol Jason,Wucherpfennig Kai W.

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference72 articles.

1. HLA-DM captures partially empty HLA-DR molecules for catalyzed removal of peptide;Anders;Nat. Immunol.,2011

2. Structural factors contributing to DM susceptibility of MHC class II/peptide complexes;Belmares;J. Immunol.,2002

3. Structure of the human class I histocompatibility antigen, HLA-A2;Bjorkman;Nature,1987

4. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1;Brown;Nature,1993

5. Secondary structure composition and pH-dependent conformational changes of soluble recombinant HLA-DM;Busch;J. Biol. Chem.,1998

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