PDBsum entry 3ff9

Immune system

PDB id

3ff9

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Contents

			Protein chains

					115 a.a. *

			Waters ×169

* Residue conservation analysis

PDB id:

3ff9

Links

Name:

Immune system

Title:

Structure of nk cell receptor klrg1

Structure:

Killer cell lectin-like receptor subfamily g member 1. Chain: a, b. Fragment: unp residues 75-188, c-type lectin domain. Synonym: mast cell function-associated antigen 2f1, mast cell function-associated antigen. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: klrg1, mafa. Expressed in: escherichia coli

Resolution:

1.80Å

R-factor:

0.223

R-free:

0.257

Authors:

Y.Li,R.A.Mariuzza

Key ref:

Y.Li et al. (2009). Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition. Immunity, 31, 35-46. PubMed id: 19604491

Date:

02-Dec-08

Release date:

28-Jul-09

PROCHECK

	Headers

	References

Protein chains

O88713 (KLRG1_MOUSE) - Killer cell lectin-like receptor subfamily G member 1 from Mus musculus

Seq: Struc:					188 a.a. 115 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

	Immunity 31:35-46 (2009)
PubMed id: 19604491

Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition.
Y.Li, M.Hofmann, Q.Wang, L.Teng, L.K.Chlewicki, H.Pircher, R.A.Mariuzza.

ABSTRACT

The cytolytic activity of natural killer (NK) cells is regulated by inhibitory receptors that detect the absence of self molecules on target cells. Structural studies of missing self recognition have focused on NK receptors that bind MHC. However, NK cells also possess inhibitory receptors specific for non-MHC ligands, notably cadherins, which are downregulated in metastatic tumors. We determined the structure of killer cell lectin-like receptor G1 (KLRG1) in complex with E-cadherin. KLRG1 mediates missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of several cadherins (E-, N-, and R-) on target cells. This site overlaps the site responsible for cell-cell adhesion but is distinct from the integrin alpha(E)beta(7) binding site. We propose that E-cadherin may coengage KLRG1 and alpha(E)beta(7) and that KLRG1 overcomes its exceptionally weak affinity for cadherins through multipoint attachment to target cells, resulting in inhibitory signaling.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20201037

C.Gründemann, S.Schwartzkopff, M.Koschella, O.Schweier, C.Peters, D.Voehringer, and H.Pircher (2010).
The NK receptor KLRG1 is dispensable for virus-induced NK and CD8+ T-cell differentiation and function in vivo.

Eur J Immunol, 40, 1303-1314.

20032175

H.P.Su, K.Singh, A.G.Gittis, and D.N.Garboczi (2010).
The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.

J Virol, 84, 2502-2510.

PDB code:

3k7b

20373518

S.Jonjic (2010).
Functional plasticity and robustness are essential characteristics of biological systems: lessons learned from KLRG1-deficient mice.

Eur J Immunol, 40, 1241-1243.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.