1nam

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(New page: 200px<br /><applet load="1nam" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nam, resolution 2.70&Aring;" /> '''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"
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[[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==
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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.
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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.
==About this Structure==
==About this Structure==
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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].
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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.]]
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[[Category: Fontecilla-Camps, J.C.]]
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[[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.]]
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[[Category: Merwe, P.A.van.der.]]
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[[Category: Merwe, P A.van der.]]
[[Category: Mosser, T.]]
[[Category: Mosser, T.]]
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[[Category: Reiser, J.B.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:05:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:00 2008''

Revision as of 12:04, 21 February 2008

Image:1nam.gif

1nam, resolution 2.70Å

Drag the structure with the mouse to rotate

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.

About this Structure

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

Reference

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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