1mpu
From Proteopedia
(New page: 200px<br /> <applet load="1mpu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mpu, resolution 2.5Å" /> '''Crystal Structure of...) |
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caption="1mpu, resolution 2.5Å" /> | caption="1mpu, resolution 2.5Å" /> | ||
'''Crystal Structure of the free human NKG2D immunoreceptor'''<br /> | '''Crystal Structure of the free human NKG2D immunoreceptor'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MPU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MPU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: c-type lectin-like domain]] | [[Category: c-type lectin-like domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:25:07 2008'' |
Revision as of 14:25, 15 February 2008
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Crystal Structure of the free human NKG2D immunoreceptor
Overview
Engagement of diverse protein ligands (MIC-A/B, ULBP, Rae-1, or H60) by, NKG2D immunoreceptors mediates elimination of tumorigenic or virally, infected cells by natural killer and T cells. Three previous NKG2D-ligand, complex structures show the homodimeric receptor interacting with the, monomeric ligands in similar 2:1 complexes, with an equivalent surface on, each NKG2D monomer binding intimately to a total of six distinct ligand, surfaces. Here, the crystal structure of free human NKG2D and in silico, and in vitro alanine-scanning mutagenesis analyses of the complex, interfaces indicate that NKG2D recognition degeneracy is not explained by, a classical induced-fit mechanism. Rather, the divergent ligands appear to, utilize different strategies to interact with structurally conserved, elements of the consensus NKG2D binding site.
About this Structure
1MPU is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Symmetry recognizing asymmetry: analysis of the interactions between the C-type lectin-like immunoreceptor NKG2D and MHC class I-like ligands., McFarland BJ, Kortemme T, Yu SF, Baker D, Strong RK, Structure. 2003 Apr;11(4):411-22. PMID:12679019
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