Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide (Q27731272)

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object named as

D C Wiley

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author name string

L J Stern

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J H Brown

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T S Jardetzky

3

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J C Gorga

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R G Urban

Molecular components of T-cell recognition

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language of work or name

English

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publication date

17 March 1994

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published in

Nature

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volume

368

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issue

6468

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page(s)

215-21

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cites work

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Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1.

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Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules

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Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry

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Identification of self peptides bound to purified HLA-B27

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Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs

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Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size

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Promiscuous and allele-specific anchors in HLA-DR-binding peptides

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The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation

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The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC

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Atomic structure of a human MHC molecule presenting an influenza virus peptide

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The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2

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Crystal structure of the major histocompatibility complex class I H-2Kb molecule containing a single viral peptide: implications for peptide binding and T-cell receptor recognition

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Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb

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The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection

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Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A*6801, HLA-A*0201, and HLA-B*2705.

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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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A hypothetical model of the foreign antigen binding site of class II histocompatibility molecules

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Common ring motifs in proteins involving asparagine or glutamine amide groups hydrogen-bonded to main-chain atoms

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Identification of a motif for HLA-DR1 binding peptides using M13 display libraries

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The set of naturally processed peptides displayed by DR molecules is tuned by polymorphism of residue 86

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HLA-DR beta chain residue 86 controls DR alpha beta dimer stability

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Position 71 in the alpha helix of the DR beta domain is predicted to influence peptide binding and plays a central role in allorecognition

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