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1mpu
From Proteopedia
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| - | [[Image:1mpu.jpg|left|200px]] | + | [[Image:1mpu.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal Structure of the free human NKG2D immunoreceptor''' | + | {{Structure |
| + | |PDB= 1mpu |SIZE=350|CAPTION= <scene name='initialview01'>1mpu</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of the free human NKG2D immunoreceptor''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MPU is a [ | + | 1MPU is a [[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=1MPU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12679019 12679019] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: c-type lectin-like domain]] | [[Category: c-type lectin-like 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 12:46:36 2008'' |
Revision as of 10:46, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 12:46:36 2008
