2clz: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:2clz.gif|left|200px]]
{{Seed}}
[[Image:2clz.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2clz|  PDB=2clz  |  SCENE=  }}  
{{STRUCTURE_2clz|  PDB=2clz  |  SCENE=  }}  


'''MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND PBM1 PEPTIDE'''
===MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND PBM1 PEPTIDE===




==Overview==
<!--  
We have characterized three different programs of activation for alloreactive CD8 T cells expressing the BM3.3 TCR, their elicitation depending on the characteristics of the stimulating peptide/MHC complex. The high-affinity interaction between the TCR and the K(b)-associated endogenous peptide pBM1 (INFDFNTI) induced a complete differentiation program into effector cells correlated with sustained ERK activation. The K(bm8) variant elicited a partial activation program with delayed T cell proliferation, poor CTL activity and undetectable ERK phosphorylation; this resulted from a low-avidity interaction of TCR BM3.3 with a newly identified endogenous peptide, pBM8 (SQYYYNSL). Interestingly, mismatched pBM1/K(bm8) complexes induced a split response in BM3.3 T cells, with total reconstitution of T cell proliferation but defective generation of CTL activity that was correlated with strong but shortened ERK phosphorylation. Crystal structures highlight the molecular basis for the higher stability of pBM8/K(bm8) compared to pBM1/K(bm8) complexes that exist in two conformers. This study illustrates the importance of the stability of both peptide/MHC and peptide/MHC-TCR interactions for induction of sustained signaling required to induce optimal CTL effector functions. Subtle allelic structural variations, amplified by peptide selection, may thus orient distinct outcomes of alloreactive TCR-based therapies.
The line below this paragraph, {{ABSTRACT_PUBMED_16761314}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16761314 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16761314}}


==About this Structure==
==About this Structure==
Line 42: Line 46:
[[Category: Polymorphism]]
[[Category: Polymorphism]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:28:02 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:18:51 2008''

Revision as of 20:18, 27 July 2008

File:2clz.png

Template:STRUCTURE 2clz

MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND PBM1 PEPTIDE

Template:ABSTRACT PUBMED 16761314

About this Structure

2CLZ is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Distinct orientation of the alloreactive monoclonal CD8 T cell activation program by three different peptide/MHC complexes., Auphan-Anezin N, Mazza C, Guimezanes A, Barrett-Wilt GA, Montero-Julian F, Roussel A, Hunt DF, Malissen B, Schmitt-Verhulst AM, Eur J Immunol. 2006 Jul;36(7):1856-66. PMID:16761314

Page seeded by OCA on Sun Jul 27 23:18:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2clz&oldid=670864"