1bwm

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(New page: 200px<br /><applet load="1bwm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bwm" /> '''A SINGLE-CHAIN T CELL RECEPTOR'''<br /> ==O...)
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'''A SINGLE-CHAIN T CELL RECEPTOR'''<br />
'''A SINGLE-CHAIN T CELL RECEPTOR'''<br />
==Overview==
==Overview==
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Using NMR spectroscopy, we determined the solution structure of a, single-chain T-cell receptor (scTCR) derived from the major, histocompatibility complex (MHC) class II-restricted D10 TCR. The, conformations of complementarity-determining regions (CDRs) 3beta and, 1alpha and surface properties of 2alpha are different from those of, related class I-restricted TCRs. We infer a conserved orientation for TCR, V(alpha) domains in complexes with both class I and II MHC-peptide, ligands, which implies that small structural variations in V(alpha) confer, MHC class preference. High mobility of CDR3 residues relative to other CDR, or framework residues (picosecond time scale) provides insight into immune, recognition and selection mechanisms.
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Using NMR spectroscopy, we determined the solution structure of a single-chain T-cell receptor (scTCR) derived from the major histocompatibility complex (MHC) class II-restricted D10 TCR. The conformations of complementarity-determining regions (CDRs) 3beta and 1alpha and surface properties of 2alpha are different from those of related class I-restricted TCRs. We infer a conserved orientation for TCR V(alpha) domains in complexes with both class I and II MHC-peptide ligands, which implies that small structural variations in V(alpha) confer MHC class preference. High mobility of CDR3 residues relative to other CDR or framework residues (picosecond time scale) provides insight into immune recognition and selection mechanisms.
==About this Structure==
==About this Structure==
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1BWM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1BWM OCA].
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1BWM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1BWM OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hare, B.J.]]
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[[Category: Hare, B J.]]
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[[Category: Reinherz, E.L.]]
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[[Category: Reinherz, E L.]]
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
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[[Category: Wyss, D.F.]]
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[[Category: Wyss, D F.]]
[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
[[Category: immunoreceptor]]
[[Category: immunoreceptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:42:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:51 2008''

Revision as of 09:59, 21 February 2008


1bwm

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A SINGLE-CHAIN T CELL RECEPTOR

Overview

Using NMR spectroscopy, we determined the solution structure of a single-chain T-cell receptor (scTCR) derived from the major histocompatibility complex (MHC) class II-restricted D10 TCR. The conformations of complementarity-determining regions (CDRs) 3beta and 1alpha and surface properties of 2alpha are different from those of related class I-restricted TCRs. We infer a conserved orientation for TCR V(alpha) domains in complexes with both class I and II MHC-peptide ligands, which implies that small structural variations in V(alpha) confer MHC class preference. High mobility of CDR3 residues relative to other CDR or framework residues (picosecond time scale) provides insight into immune recognition and selection mechanisms.

About this Structure

1BWM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure, specificity and CDR mobility of a class II restricted single-chain T-cell receptor., Hare BJ, Wyss DF, Osburne MS, Kern PS, Reinherz EL, Wagner G, Nat Struct Biol. 1999 Jun;6(6):574-81. PMID:10360364

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