2dli
From Proteopedia
(New page: 200px<br /> <applet load="2dli" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dli, resolution 2.9Å" /> '''KILLER IMMUNOGLOBULI...) |
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caption="2dli, resolution 2.9Å" /> | caption="2dli, resolution 2.9Å" /> | ||
'''KILLER IMMUNOGLOBULIN RECEPTOR 2DL2,TRIGONAL FORM'''<br /> | '''KILLER IMMUNOGLOBULIN RECEPTOR 2DL2,TRIGONAL FORM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2DLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2DLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DLI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: natural killer receptor]] | [[Category: natural killer receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:20:55 2008'' |
Revision as of 15:20, 15 February 2008
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KILLER IMMUNOGLOBULIN RECEPTOR 2DL2,TRIGONAL FORM
Overview
Killer cell inhibitory receptors (KIR) protect class I HLAs expressing, target cells from natural killer (NK) cell-mediated lysis. To understand, the molecular basis of this receptor-ligand recognition, we have, crystallized the extracellular ligand-binding domains of KIR2DL2, a member, of the Ig superfamily receptors that recognize HLA-Cw1, 3, 7, and 8, allotypes. The structure was determined in two different crystal forms, an, orthorhombic P212121 and a trigonal P3221 space group, to resolutions of, 3.0 and 2.9 A, respectively. The overall fold of this structure, like, KIR2DL1, exhibits K-type Ig topology with cis-proline residues in both, domains that define beta-strand switching, which sets KIR apart from the, C2-type hematopoietic growth hormone receptor fold. The hinge angle of, KIR2DL2 is approximately 80 degrees, 14 degrees larger than that observed, in KIR2DL1 despite the existence of conserved hydrophobic residues near, the hinge region. There is also a 5 degrees difference in the observed, hinge angles in two crystal forms of 2DL2, suggesting that the interdomain, hinge angle is not fixed. The putative ligand-binding site is formed by, residues from several variable loops with charge distribution apparently, complementary to that of HLA-C. The packing of the receptors in the, orthorhombic crystal form offers an intriguing model for receptor, aggregation on the cell surface.
About this Structure
2DLI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2., Snyder GA, Brooks AG, Sun PD, Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3864-9. PMID:10097129
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