1ac6
From Proteopedia
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| - | [[Image:1ac6.jpg|left|200px]] | + | [[Image:1ac6.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF A VARIABLE DOMAIN MUTANT OF A T-CELL RECEPTOR ALPHA CHAIN''' | + | {{Structure |
| + | |PDB= 1ac6 |SIZE=350|CAPTION= <scene name='initialview01'>1ac6</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF A VARIABLE DOMAIN MUTANT OF A T-CELL RECEPTOR ALPHA CHAIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AC6 is a [ | + | 1AC6 is a [[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=1AC6 OCA]. |
==Reference== | ==Reference== | ||
| - | Dual conformations of a T cell receptor V alpha homodimer: implications for variability in V alpha V beta domain association., Li H, Lebedeva MI, Ward ES, Mariuzza RA, J Mol Biol. 1997 Jun 13;269(3):385-94. PMID:[http:// | + | Dual conformations of a T cell receptor V alpha homodimer: implications for variability in V alpha V beta domain association., Li H, Lebedeva MI, Ward ES, Mariuzza RA, J Mol Biol. 1997 Jun 13;269(3):385-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9199407 9199407] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: v alpha domain]] | [[Category: v alpha domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:55:38 2008'' |
Revision as of 07:55, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A VARIABLE DOMAIN MUTANT OF A T-CELL RECEPTOR ALPHA CHAIN
Overview
The crystal structure of a mutant T cell receptor (TCR) V alpha domain containing a grafted third complementarity-determining region (CDR3) from a different V alpha was determined at 2.3 A resolution by molecular replacement using the wild-type V alpha structure as a search model. Like the wild-type V alpha domain, the mutant crystallized as a homodimer very similar to TCR V alpha V beta and antibody V(L)V(H) heterodimers, with the CDR loops disposed to form part of the antigen-binding site. However, the relative orientation of the two chains in the mutant V alpha homodimer differs from that in the wild-type by a rotation of 14 degrees such that the buried surface area in the dimer interface of the mutant is 140 A2 less than in the wild-type. While the residues forming the interface are essentially the same in the two structures, there are only four pairs of interface hydrogen bonds in the case of the mutant compared with eight for the wild-type. These results suggest that multiple relative orientations of the V alpha and V beta domains of TCRs may be possible, providing a significant contribution to TCR combining site diversity.
About this Structure
1AC6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Dual conformations of a T cell receptor V alpha homodimer: implications for variability in V alpha V beta domain association., Li H, Lebedeva MI, Ward ES, Mariuzza RA, J Mol Biol. 1997 Jun 13;269(3):385-94. PMID:9199407
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