PDBsum entry: 1hq8

Apoptosis

PDB id: 1hq8

Contents

Protein chain

123 a.a. *

Waters ×77

* Residue conservation analysis

PDB id:

1hq8

Name:

Apoptosis

Title:

Crystal structure of the murine nk cell-activating receptor nkg2d at 1.95 a

Structure:

Nkg2-d. Chain: a. Fragment: extracellular domain. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PDB file)

Resolution:

1.95Å R-factor: 0.215 R-free: 0.227

Authors:

D.W.Wolan,L.Teyton,M.G.Rudolph,B.Villmow,S.Bauer,D.H.Busch, I.A.Wilson

Key ref:

D.W.Wolan et al. (2001). Crystal structure of the murine NK cell-activating receptor NKG2D at 1.95 A. Nat Immunol, 2, 248-254. PubMed id: 11224525 DOI: 10.1038/85311

Date:

14-Dec-00 Release date: 07-Mar-01

Protein chain

O54709  (NKG2D_MOUSE) -  NKG2-D type II integral membrane protein

Seq: 232 a.a.

Struc: 123 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: binding (2 terms)

DOI no: 10.1038/85311

Nat Immunol 2:248-254 (2001)

PubMed id: 11224525

Crystal structure of the murine NK cell-activating receptor NKG2D at 1.95 A.

D.W.Wolan, L.Teyton, M.G.Rudolph, B.Villmow, S.Bauer, D.H.Busch, I.A.Wilson.

ABSTRACT

NKG2D, a homodimeric lectin-like receptor, is a unique stimulatory molecule that is found on natural killer cells,T cells and activated macrophages.The natural ligands for murine NKG2D are distant major histocompatibility complex homologs, retinoic acid early transcript (Rae1) and H-60 minor histocompatibility antigen. The crystal structure of the extracellular region of murine NKG2D reveals close homology with other C-type lectin receptors such as CD94, Ly49A, rat MBP-A and CD69. However, the precise mode of dimeric assembly varies among these natural killer receptors, as well as their surface topography and electrostatic properties.The NKG2D structure provides the first structural insights into the role and ligand specificity of this stimulatory receptor in the innate and adaptive immune system.

Selected figure(s)

Figure 2.
Figure 2. Structure of the murine NKG2D homodimer. (a) Top view looking down onto the proposed binding surface. (b) Side view showing the NH[2] terminus at the bottom of the structure that would connect to the membrane at the cell surface by a stalk comprised of 16 residues. The dimer is formed primarily of an extension of the first -sheet ( 1) across the interface. Color-coding as for Fig. 1.

Figure 4.
Figure 4. Comparison of disulfide bridges at the dimer interfaces of NKG2D, CD94 and Ly49A. Color-coding as for Fig. 3. Cysteines are colored yellow (for carbon) and green (for sulfur).

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Immunol (2001, 2, 248-254) copyright 2001.

Figures were selected by an automated process.