1nan: Difference between revisions

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New page: left|200px<br /><applet load="1nan" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nan, resolution 2.30Å" /> '''MCH CLASS I H-2KB MO...
 
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[[Image:1nan.gif|left|200px]]<br /><applet load="1nan" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1nan.gif|left|200px]]<br /><applet load="1nan" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1nan, resolution 2.30&Aring;" />
caption="1nan, resolution 2.30&Aring;" />
'''MCH CLASS I H-2KB MOLECULE COMPLEXED WITH PBM1 PEPTIDE'''<br />
'''MCH CLASS I H-2KB MOLECULE COMPLEXED WITH PBM1 PEPTIDE'''<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==
1NAN 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=1NAN OCA].  
1NAN 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=1NAN 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: h-2kb]]
[[Category: h-2kb]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:06:03 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:07 2008''

Revision as of 15:04, 21 February 2008

File:1nan.gif


1nan, resolution 2.30Å

Drag the structure with the mouse to rotate

MCH CLASS I H-2KB MOLECULE COMPLEXED WITH PBM1 PEPTIDE

OverviewOverview

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 StructureAbout this Structure

1NAN is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

CDR3 loop flexibility contributes to the degeneracy of TCR recognition., Reiser JB, Darnault C, Gregoire C, Mosser T, Mazza G, Kearney A, van der Merwe PA, Fontecilla-Camps JC, Housset D, Malissen B, Nat Immunol. 2003 Mar;4(3):241-7. Epub 2003 Feb 3. PMID:12563259

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