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.

2a83

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2a83.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2a83.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2a83| PDB=2a83 | SCENE= }}
{{STRUCTURE_2a83| PDB=2a83 | SCENE= }}
-
'''Crystal structure of hla-b*2705 complexed with the glucagon receptor (gr) peptide (residues 412-420)'''
+
===Crystal structure of hla-b*2705 complexed with the glucagon receptor (gr) peptide (residues 412-420)===
-
==Overview==
+
<!--
-
An interesting property of certain peptides presented by major histocompatibility complex (MHC) molecules is their acquisition of a dual binding mode within the peptide binding groove. Using x-ray crystallography at 1.4 A resolution, we show here that the glucagon receptor-derived self-peptide pGR ((412)RRRWHRWRL(420)) is presented by the disease-associated human MHC class I subtype HLA-B*2705 in a dual conformation as well, with the middle of the peptide bent toward the floor of the peptide binding groove of the molecule in both binding modes. The conformations of pGR are compared here with those of another self-peptide (pVIPR, RRKWRRWHL) that is also displayed in two binding modes by HLA-B*2705 antigens and with that of the viral peptide pLMP2 (RRRWRRLTV). Conserved structural features suggest that the N-terminal halves of the peptides are crucial in allowing cytotoxic T lymphocyte (CTL) cross-reactivity. In addition, an analysis of T cell receptors (TCRs) from pGR- or pVIPR-directed, HLA-B27-restricted CTL clones demonstrates that TCR from distinct clones but with comparable reactivity may share CDR3alpha but not CDR3beta regions. Therefore, the cross-reactivity of these CTLs depends on TCR-CDR3alpha, is modulated by TCR-CDR3beta sequences, and is ultimately a consequence of the conformational dimorphism that characterizes binding of the self-peptides to HLA-B*2705. These results lend support to the concept that conformational dimorphisms of MHC class I-bound peptides might be connected with the occurrence of self-reactive CTL.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16221670}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16221670 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16221670}}
==Disease==
==Disease==
Line 35: Line 39:
[[Category: Ziegler, A.]]
[[Category: Ziegler, A.]]
[[Category: Immune system]]
[[Category: Immune system]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:43:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:17:10 2008''

Revision as of 21:17, 27 July 2008

Image:2a83.png

Template:STRUCTURE 2a83

Contents

Crystal structure of hla-b*2705 complexed with the glucagon receptor (gr) peptide (residues 412-420)

Template:ABSTRACT PUBMED 16221670

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

2A83 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational dimorphism of self-peptides and molecular mimicry in a disease-associated HLA-B27 subtype., Ruckert C, Fiorillo MT, Loll B, Moretti R, Biesiadka J, Saenger W, Ziegler A, Sorrentino R, Uchanska-Ziegler B, J Biol Chem. 2006 Jan 27;281(4):2306-16. Epub 2005 Oct 12. PMID:16221670

Page seeded by OCA on Mon Jul 28 00:17:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a83"
Personal tools