1p4l
From Proteopedia
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|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]), KLRA3 OR LY49C OR LY-49C ([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]), KLRA3 OR LY49C OR LY-49C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1p1z|1P1Z]], [[1vac|1VAC]], [[1qo3|1QO3]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4l OCA], [http://www.ebi.ac.uk/pdbsum/1p4l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p4l RCSB]</span> | ||
}} | }} | ||
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[[Category: natural killer receptor]] | [[Category: natural killer receptor]] | ||
| - | ''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 22:54:45 2008'' |
Revision as of 19:54, 30 March 2008
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| , resolution 2.90Å | |||||||
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| Gene: | H2-K (Mus musculus), B2M (Mus musculus), KLRA3 OR LY49C OR LY-49C (Mus musculus) | ||||||
| Related: | 1P1Z, 1VAC, 1QO3
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb
Overview
The Ly49 family of natural killer (NK) receptors regulates NK cell function by sensing major histocompatibility complex (MHC) class I. Ly49 receptors show complex patterns of MHC class I cross-reactivity and, in certain cases, peptide selectivity. To investigate whether specificity differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules in symmetrical way, a mode distinct from that of Ly49A, which binds MHC class I asymmetrically. Ly49C does not directly contact the MHC-bound peptide. In addition, MHC crosslinking by Ly49C was demonstrated in solution. We propose a dynamic model for Ly49-MHC class I interactions involving conformational changes in the receptor, whereby variations in Ly49 dimerization mediate different MHC-binding modes.
About this Structure
1P4L is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b)., Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA, Nat Immunol. 2003 Dec;4(12):1213-22. Epub 2003 Nov 2. PMID:14595439
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