1mpu: Difference between revisions

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[[Image:1mpu.jpg|left|200px]]
[[Image:1mpu.jpg|left|200px]]


{{Structure
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{{STRUCTURE_1mpu|  PDB=1mpu |  SCENE= }}  
|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>
}}


'''Crystal Structure of the free human NKG2D immunoreceptor'''
'''Crystal Structure of the free human NKG2D immunoreceptor'''
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[[Category: McFarland, B J.]]
[[Category: McFarland, B J.]]
[[Category: Strong, R K.]]
[[Category: Strong, R K.]]
[[Category: c-type lectin-like domain]]
[[Category: C-type lectin-like domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:34:16 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:29 2008''

Revision as of 01:34, 3 May 2008

File:1mpu.jpg

Template:STRUCTURE 1mpu

Crystal Structure of the free human NKG2D immunoreceptor


OverviewOverview

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 StructureAbout this Structure

1MPU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Sat May 3 01:34:16 2008

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