› 2frg

X-ray diffraction
1.19Å resolution

Structure of the immunoglobulin-like domain of human TLT-1

Released:
DOI: 10.2210/pdb2frg/pdb
PDB entry 2frg coloured by chain, front view.
PDB entry 2frg coloured by chain, side view.
PDB entry 2frg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of the extracellular domain of triggering receptor expressed on myeloid cells like transcript-1 and evidence for a naturally occurring soluble fragment.
Gattis JL, Washington AV, Chisholm MM, Quigley L, Szyk A, McVicar DW, Lubkowski J
J Biol Chem 281 13396-13403 (2006)
PMID: 16505478

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183281 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trem-like transcript 1 protein Chain: P
Molecule details ›
Chain: P
Length: 106 amino acids
Theoretical weight: 11.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86YW5 (Residues: 20-125; Coverage: 36%)
Gene names: TLT1, TREML1, UNQ1825/PRO3438
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 47.095Å b: 79.981Å c: 25.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.176 0.191
Expression system: Escherichia coli

Quick links

Citations

13 review citations

The TREM receptor family and signal integration.
Klesney-Tait et al. (2006)
12 more

3 mentions without citation

Neurodegenerative disease mutations in TREM2 reveal a functional surface and distinct loss-of-function mechanisms.
Kober et al. (2016)
2 more