1nam: Difference between revisions

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~~'''~~MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX~~'''~~

===MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX===

~~==Overview==~~

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~~T cell receptor (TCR) binding degeneracy lies at the heart of several physiological and pathological phenomena~~, ~~yet its structural basis is poorly understood. We determined the crystal structure of a complex involving~~ the ~~BM3.3 TCR and an octapeptide (VSV8) bound~~ to the ~~H-2K~~(~~b) major histocompatibility complex molecule~~ at ~~a 2~~.~~7 A resolution, and compared it with the BM3~~.~~3 TCR bound to the H-2K(b~~) ~~molecule loaded with a peptide that has no primary sequence identity with VSV8. Comparison of these structures showed that~~ the ~~BM3~~.~~3 TCR complementarity~~-~~determining region (CDR) 3alpha could undergo rearrangements to adapt to structurally different peptide residues. Therefore, CDR3 loop flexibility helps explain TCR binding cross~~-~~reactivity.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12563259}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12563259 is the PubMed ID number.

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==About this Structure==

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[[Category: T cell receptor]]

[[Category: Tcr-pmhc complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:17:56 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:23:21 2008''

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-[[Image:1nam.gif|left|200px]]
+{{Seed}}
+[[Image:1nam.png|left|200px]]
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 {{STRUCTURE_1nam|  PDB=1nam  |  SCENE=  }}
-'''MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX'''
+===MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX===
-==Overview==
+<!--
-T cell receptor (TCR) binding degeneracy lies at the heart of several physiological and pathological phenomena, yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and an octapeptide (VSV8) bound to the H-2K(b) major histocompatibility complex molecule at a 2.7 A resolution, and compared it with the BM3.3 TCR bound to the H-2K(b) molecule loaded with a peptide that has no primary sequence identity with VSV8. Comparison of these structures showed that the BM3.3 TCR complementarity-determining region (CDR) 3alpha could undergo rearrangements to adapt to structurally different peptide residues. Therefore, CDR3 loop flexibility helps explain TCR binding cross-reactivity.
+The line below this paragraph, {{ABSTRACT_PUBMED_12563259}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12563259 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12563259}}
 ==About this Structure==
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 [[Category: T cell receptor]]
 [[Category: Tcr-pmhc complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:17:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:23:21 2008''