Determinants of the peptide-induced conformational change in the human class II major histocompatibility complex protein HLA-DR1. (Q42617265)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10636922%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

title

Determinants of the peptide-induced conformational change in the human class II major histocompatibility complex protein HLA-DR1 (English)

1 reference

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3 November 2019

author name string

A K Sato

1

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3 November 2019

J A Zarutskie

2

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3 November 2019

M M Rushe

3

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3 November 2019

A Lomakin

4

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3 November 2019

S K Natarajan

5

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3 November 2019

L J Stern

8

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3 November 2019

language of work or name

English

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publication date

1 January 2000

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Journal of Biological Chemistry

3 November 2019

published in

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3 November 2019

volume

275

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3 November 2019

issue

3

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3 November 2019

page(s)

2165-2173

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MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation

3 November 2019

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Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues

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Stability of empty and peptide-loaded class II major histocompatibility complex molecules at neutral and endosomal pH: comparison to class I proteins

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A structural transition in class II major histocompatibility complex proteins at mildly acidic pH.

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Evidence for a conformational change in a class II major histocompatibility complex molecule occurring in the same pH range where antigen binding is enhanced

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HLA-DM induces CLIP dissociation from MHC class II alpha beta dimers and facilitates peptide loading

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Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro.

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The human class II MHC protein HLA-DR1 assembles as empty alpha beta heterodimers in the absence of antigenic peptide

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