1h5b
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(New page: 200px<br /><applet load="1h5b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h5b, resolution 1.85Å" /> '''T CELL RECEPTOR VALP...)
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Revision as of 00:05, 25 November 2007
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T CELL RECEPTOR VALPHA11 (AV11S5) DOMAIN
Overview
We describe the X-ray crystallographic structure of a murine T cell, receptor (TCR) Valpha domain ("Valpha85.33"; AV11S5-AJ17) to 1.85 A, resolution. The Valpha85.33 domain is derived from a TCR that recognizes a, type II collagen peptide associated with the murine major, histocompatibility complex (MHC) class II molecule, I-A(q). Valpha85.33, packs as a Valpha-Valpha homodimer with a highly symmetric monomer-monomer, interface. The first and second complementarity determining regions (CDR1, and CDR2) of this Valpha are shorter than the CDRs corresponding to the, majority of other Valpha gene families, and three-dimensional structures, of CDRs of these lengths have not been described previously. The CDR1 and, CDR2 therefore represent new canonical forms that could serve as templates, for AV11 family members. CDR3 of the Valpha85.33 domain is highly flexible, and this is consistent with plasticity of this region of the TCR. The, fourth hypervariable loop (HV4alpha) of AV11 and AV10 family members is, one residue longer than that of other HV4alpha regions and shows a high, degree of flexibility. The increase in length results in a distinct, disposition of the conserved residue Lys68, which has been shown in other, studies to play a role in antigen recognition. The X-ray structure of, Valpha85.33 extends the database of canonical forms for CDR1 and CDR2, and, has implications for antigen recognition by TCRs that contain related, Valpha domains.
About this Structure
1H5B is a Single protein structure of sequence from Mus musculus with CL and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a T cell receptor Valpha11 (AV11S5) domain: new canonical forms for the first and second complementarity determining regions., Machius M, Cianga P, Deisenhofer J, Ward ES, J Mol Biol. 2001 Jul 20;310(4):689-98. PMID:11453680
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