We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1j8h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1j8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j8h, resolution 2.40&Aring;" /> '''Crystal Structure o...)
Next diff →

Revision as of 15:31, 12 November 2007


1j8h, resolution 2.40Å

Drag the structure with the mouse to rotate

Crystal Structure of a Complex of a Human alpha/beta-T cell Receptor, Influenza HA Antigen Peptide, and MHC Class II Molecule, HLA-DR4

Overview

The alpha/beta T cell receptor (TCR) HA1.7 specific for the hemagglutinin, (HA) antigen peptide from influenza A virus is HLA-DR1 restricted but, cross-reactive for the HA peptide presented by the allo-major, histocompatibility complex (MHC) class II molecule HLA-DR4. We report here, the structure of the HA1.7/DR4/HA complex, determined by X-ray, crystallography at a resolution of 2.4 A. The overall structure of this, complex is very similar to the previously reported structure of the, HA1.7/DR1/HA complex. Amino acid sequence differences between DR1 and DR4, which are located deep in the peptide binding groove and out of reach for, direct contact by the TCR, are able to indirectly influence the, antigenicity of the pMHC surface by changing the conformation of HA, peptide residues at position P5 and P6. Although TCR HA1.7 is, cross-reactive for HA presented by DR1 and DR4 and tolerates these, conformational differences, other HA-specific TCRs are sensitive to these, changes. We also find a dependence of the width of the MHC class II, peptide-binding groove on the sequence of the bound peptide by comparing, the HA1.7/DR4/HA complex with the structure of DR4 presenting a collagen, peptide. This structural study of TCR cross-reactivity emphasizes how MHC, sequence differences can affect TCR binding indirectly by moving peptide, atoms.

About this Structure

1J8H is a Protein complex structure of sequences from Homo sapiens and Influenzavirus a with NAG and NDG as ligands. Full crystallographic information is available from OCA.

Reference

Structure of a complex of the human alpha/beta T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA*0101 and DRB1*0401): insight into TCR cross-restriction and alloreactivity., Hennecke J, Wiley DC, J Exp Med. 2002 Mar 4;195(5):571-81. PMID:11877480

Page seeded by OCA on Mon Nov 12 17:38:23 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools