1MPU

Crystal Structure of the free human NKG2D immunoreceptor

Summary for 1MPU

• Entry DOI: 10.2210/pdb1mpu/pdb
• Related: 1HQ8 1HYR 1JSK 1KCG
• Descriptor: NKG2-D type II integral membrane protein, PHOSPHATE ION (3 entities in total)
• Functional Keywords: c-type lectin-like domain, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Single- pass type II membrane protein : P26718
• Total number of polymer chains: 1
• Total formula weight: 16076.07

Authors

McFarland, B.J.,Kortemme, T.,Baker, D.,Strong, R.K. (deposition date: 2002-09-12, release date: 2003-04-15, Last modification date: 2024-11-13)

Primary citation

McFarland, B.J.,Kortemme, T.,Yu, S.F.,Baker, D.,Strong, R.K.
Symmetry Recognizing Asymmetry: Analysis of the Interactions between the C-Type Lectin-like Immunoreceptor NKG2D and MHC Class I-like Ligands
Structure, 11:411-422, 2003

PubMed Abstract: 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.

PubMed: 12679019
DOI: 10.1016/S0969-2126(03)00047-9

Experimental method

X-RAY DIFFRACTION (2.5 Å)