1nam: Difference between revisions

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New page: left|200px<br /><applet load="1nam" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nam, resolution 2.70Å" /> '''MURINE ALLOREACTIVE ...
 
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[[Image:1nam.gif|left|200px]]<br /><applet load="1nam" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1nam.gif|left|200px]]<br /><applet load="1nam" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1nam, resolution 2.70&Aring;" />
caption="1nam, resolution 2.70&Aring;" />
'''MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX'''<br />
'''MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX'''<br />


==Overview==
==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.
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.


==About this Structure==
==About this Structure==
1NAM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NAM OCA].  
1NAM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAM OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Darnault, C.]]
[[Category: Darnault, C.]]
[[Category: Fontecilla-Camps, J.C.]]
[[Category: Fontecilla-Camps, J C.]]
[[Category: Gregoire, C.]]
[[Category: Gregoire, C.]]
[[Category: Housset, D.]]
[[Category: Housset, D.]]
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[[Category: Malissen, B.]]
[[Category: Malissen, B.]]
[[Category: Mazza, G.]]
[[Category: Mazza, G.]]
[[Category: Merwe, P.A.van.der.]]
[[Category: Merwe, P A.van der.]]
[[Category: Mosser, T.]]
[[Category: Mosser, T.]]
[[Category: Reiser, J.B.]]
[[Category: Reiser, J B.]]
[[Category: alloreactivity]]
[[Category: alloreactivity]]
[[Category: class i mhc]]
[[Category: class i mhc]]
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[[Category: tcr-pmhc complex]]
[[Category: tcr-pmhc complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:05:58 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:00 2008''