1mpu
From Proteopedia
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|PDB= 1mpu |SIZE=350|CAPTION= <scene name='initialview01'>1mpu</scene>, resolution 2.5Å | |PDB= 1mpu |SIZE=350|CAPTION= <scene name='initialview01'>1mpu</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hyr|1HYR]], [[1kcg|1KCG]], [[1hq8|1HQ8]], [[1jsk|1JSK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpu OCA], [http://www.ebi.ac.uk/pdbsum/1mpu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mpu RCSB]</span> | ||
}} | }} | ||
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[[Category: McFarland, B J.]] | [[Category: McFarland, B J.]] | ||
[[Category: Strong, R K.]] | [[Category: Strong, R K.]] | ||
| - | [[Category: PO4]] | ||
[[Category: c-type lectin-like domain]] | [[Category: c-type lectin-like domain]] | ||
| - | ''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 22:19:29 2008'' |
Revision as of 19:19, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1HYR, 1KCG, 1HQ8, 1JSK
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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