1nam
From Proteopedia
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|PDB= 1nam |SIZE=350|CAPTION= <scene name='initialview01'>1nam</scene>, resolution 2.70Å | |PDB= 1nam |SIZE=350|CAPTION= <scene name='initialview01'>1nam</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= H2-K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= H2-K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1fo0|1FO0]], [[1kj3|1KJ3]], [[2vaa|2VAA]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nam OCA], [http://www.ebi.ac.uk/pdbsum/1nam PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nam RCSB]</span> | ||
}} | }} | ||
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[[Category: tcr-pmhc complex]] | [[Category: tcr-pmhc complex]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:27:40 2008'' |
Revision as of 19:27, 30 March 2008
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, resolution 2.70Å | |||||||
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Ligands: | |||||||
Gene: | H2-K (Mus musculus), B2M (Mus musculus) | ||||||
Related: | 1FO0, 1KJ3, 2VAA
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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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