1m05: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1m05.gif|left|200px]]
{{Seed}}
[[Image:1m05.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m05|  PDB=1m05  |  SCENE=  }}  
{{STRUCTURE_1m05|  PDB=1m05  |  SCENE=  }}  


'''HLA B8 in complex with an Epstein Barr Virus determinant'''
===HLA B8 in complex with an Epstein Barr Virus determinant===




==Overview==
<!--
EBV is a ubiquitous human pathogen that chronically infects up to 90% of the population. Persistent viral infection is characterized by latency and periods of viral replication that are kept in check by a strong antiviral CTL response. Despite the size of the EBV genome, CTL immunity focuses on only a few viral determinants but expands a large primary and memory response toward these epitopes. In unrelated HLA-B8(+) individuals, the response to the immunodominant latent Ag FLRGRAYGL from Epstein Barr nuclear Ag 3A is largely comprised of CTL clones with identical conserved alphabeta TCR structures. To better understand the structural correlates of Ag immunodominance and TCR selection bias, we have solved the crystal structure of the HLA-B8-FLRGRAYGL peptide complex to a resolution of 1.9 A. The structure confirms the importance of P3-Arg, P5-Arg, and P9-Leu as dominant anchor residues involved in peptide binding to HLA-B8. A bulged conformation of the bound peptide provides a structural basis for the critical role of the P7-Tyr residue in T cell recognition. The peptide also induces backbone and side-chain conformational changes in HLA-B8 that are transmitted along the peptide-binding groove in a domino effect. The HLA-B8-FLRGRAYGL complex crystallizes as a dimer in the asymmetric unit and is oriented such that both peptide ligands are projected in the same plane suggesting a higher order arrangement of MHC-peptide complexes that could be involved in formation of the class I Ag-loading complex or in T cell activation.
The line below this paragraph, {{ABSTRACT_PUBMED_12391232}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12391232 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12391232}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Hla b8]]
[[Category: Hla b8]]
[[Category: Mhc class i]]
[[Category: Mhc class i]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:28:26 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:55:38 2008''

Revision as of 19:55, 2 July 2008

File:1m05.png

Template:STRUCTURE 1m05

HLA B8 in complex with an Epstein Barr Virus determinant

Template:ABSTRACT PUBMED 12391232

About this Structure

1M05 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structure of HLA-B8 complexed to an immunodominant viral determinant: peptide-induced conformational changes and a mode of MHC class I dimerization., Kjer-Nielsen L, Clements CS, Brooks AG, Purcell AW, Fontes MR, McCluskey J, Rossjohn J, J Immunol. 2002 Nov 1;169(9):5153-60. PMID:12391232

Page seeded by OCA on Wed Jul 2 22:55:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1m05&oldid=628338"