PDBsum entry 1q8m

Immune system receptor

PDB id: 1q8m

Contents

Protein chains

121 a.a. *

Ligands

SO4 ×10

GSH

Waters ×159

* Residue conservation analysis

PDB id:

1q8m

Name:

Immune system receptor

Title:

Crystal structure of the human myeloid cell activating receptor trem-1

Structure:

Triggering receptor expressed on myeloid cells 1. Chain: a, b, c, d. Fragment: extracellular domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: trem1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PQS)

Resolution:

2.60Å R-factor: 0.201 R-free: 0.251

Authors:

S.Radaev,M.Kattah,B.Rostro,M.Colonna,P.D.Sun

Key ref:

S.Radaev et al. (2003). Crystal structure of the human myeloid cell activating receptor TREM-1. Structure, 11, 1527-1535. PubMed id: 14656437 DOI: 10.1016/j.str.2003.11.001

Date:

21-Aug-03 Release date: 09-Dec-03

Protein chains

Q9NP99  (TREM1_HUMAN) -  Triggering receptor expressed on myeloid cells 1 from Homo sapiens

Seq: 234 a.a.

Struc: 121 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/j.str.2003.11.001

Structure 11:1527-1535 (2003)

PubMed id: 14656437

Crystal structure of the human myeloid cell activating receptor TREM-1.

S.Radaev, M.Kattah, B.Rostro, M.Colonna, P.D.Sun.

ABSTRACT

Triggering receptors expressed on myeloid cells (TREM) are a family of recently discovered receptors that play important roles in innate immune responses, such as to activate inflammatory responses and to contribute to septic shock in response to microbial-mediated infections. To date, two TREM receptors in human and several homologs in mice have been identified. We report the 2.6 A resolution crystal structure of the extracellular domain of human TREM-1. The overall fold of the receptor resembles that of a V-type immunoglobulin domain with differences primarily located in the N-terminal strand. TREM-1 forms a "head-to-tail" dimer with 4100 A(2) interface area that is partially mediated by a domain swapping between the first strands. This mode of dimer formation is different from the "head-to-head" dimerization that existed in V(H)V(L) domains of antibodies or V domains of T cell receptors. As a result, the dimeric TREM-1 most likely contains two distinct ligand binding sites.

Selected figure(s)

Figure 2.
Figure 2. TREM-1 Dimer Interfaces(A) Stereoview of TREM-1 dimer. Secondary structure elements involved in the interactions between N termini painted green in one monomer and yellow in another one.(B) Detailed view of the hydrophobic core formed at the dimer interface by the N termini of TREM-1.(C) Interactions between CC' regions of the monomers.(D) Major interactions holding the two dimers. Residues participating in binding are shown as ball-and-sticks, color coded by strand color, except for oxygen (red), nitrogen (blue), and sulfur (yellow).

The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 1527-1535) copyright 2003.

Figure was selected by an automated process.