1i9e

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(New page: 200px<br /><applet load="1i9e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i9e, resolution 2.50&Aring;" /> '''TCR DOMAIN'''<br /> ...)
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[[Image:1i9e.jpg|left|200px]]<br /><applet load="1i9e" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1i9e.jpg|left|200px]]<br /><applet load="1i9e" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1i9e, resolution 2.50&Aring;" />
caption="1i9e, resolution 2.50&Aring;" />
'''TCR DOMAIN'''<br />
'''TCR DOMAIN'''<br />
==Overview==
==Overview==
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The T-cell receptor (TCR) is a heterodimeric cell-surface protein, consisting of two chains, alpha and beta, each of which is composed of a, variable (V) and a constant (C) domain. Crystals of the isolated V(alpha), domain of the murine TCR 2C were grown by serendipity from a solution, containing the extracellular domains of the intact TCR 2C and CD3 gamma, epsilon-chains. The V(alpha) crystal structure shows how crystal packing, can substitute for another V(alpha) domain in a different fashion from, that observed in V(alpha)/V(alpha) homodimer and V(alpha)/V(beta), heterodimer structures. Significant conformational changes occur in the, CDR3 and beta(3)beta(4) loops that normally form part of the dimer, interface. The monomeric V(alpha) domain provides the unique opportunity, to study the effect of dimerization on the conformation of the unliganded, complementarity-determining regions (CDR) of a TCR. This structure of an, individual V(alpha) module has implications for stability and, bioengineering of isolated antibody and immunoglobulin domains.
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The T-cell receptor (TCR) is a heterodimeric cell-surface protein consisting of two chains, alpha and beta, each of which is composed of a variable (V) and a constant (C) domain. Crystals of the isolated V(alpha) domain of the murine TCR 2C were grown by serendipity from a solution containing the extracellular domains of the intact TCR 2C and CD3 gamma epsilon-chains. The V(alpha) crystal structure shows how crystal packing can substitute for another V(alpha) domain in a different fashion from that observed in V(alpha)/V(alpha) homodimer and V(alpha)/V(beta) heterodimer structures. Significant conformational changes occur in the CDR3 and beta(3)beta(4) loops that normally form part of the dimer interface. The monomeric V(alpha) domain provides the unique opportunity to study the effect of dimerization on the conformation of the unliganded complementarity-determining regions (CDR) of a TCR. This structure of an individual V(alpha) module has implications for stability and bioengineering of isolated antibody and immunoglobulin domains.
==About this Structure==
==About this Structure==
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1I9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I9E OCA].
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1I9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9E OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Huang, M.]]
[[Category: Huang, M.]]
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[[Category: Rudolph, M.G.]]
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[[Category: Rudolph, M G.]]
[[Category: Teyton, L.]]
[[Category: Teyton, L.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: ig-like domain]]
[[Category: ig-like domain]]
[[Category: t cell receptor]]
[[Category: t cell receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:11:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:23 2008''

Revision as of 11:09, 21 February 2008


1i9e, resolution 2.50Å

Drag the structure with the mouse to rotate

TCR DOMAIN

Overview

The T-cell receptor (TCR) is a heterodimeric cell-surface protein consisting of two chains, alpha and beta, each of which is composed of a variable (V) and a constant (C) domain. Crystals of the isolated V(alpha) domain of the murine TCR 2C were grown by serendipity from a solution containing the extracellular domains of the intact TCR 2C and CD3 gamma epsilon-chains. The V(alpha) crystal structure shows how crystal packing can substitute for another V(alpha) domain in a different fashion from that observed in V(alpha)/V(alpha) homodimer and V(alpha)/V(beta) heterodimer structures. Significant conformational changes occur in the CDR3 and beta(3)beta(4) loops that normally form part of the dimer interface. The monomeric V(alpha) domain provides the unique opportunity to study the effect of dimerization on the conformation of the unliganded complementarity-determining regions (CDR) of a TCR. This structure of an individual V(alpha) module has implications for stability and bioengineering of isolated antibody and immunoglobulin domains.

About this Structure

1I9E is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of an isolated V(alpha) domain of the 2C T-cell receptor., Rudolph MG, Huang M, Teyton L, Wilson IA, J Mol Biol. 2001 Nov 16;314(1):1-8. PMID:11724527

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