› 1gpz

X-ray diffraction
2.9Å resolution

THE CRYSTAL STRUCTURE OF THE ZYMOGEN CATALYTIC DOMAIN OF COMPLEMENT PROTEASE C1R

Released:
DOI: 10.2210/pdb1gpz/pdb
PDB entry 1gpz coloured by chain, front view.
PDB entry 1gpz coloured by chain, side view.
PDB entry 1gpz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex.
Budayova-Spano M, Lacroix M, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C
EMBO J 21 231-9 (2002)
PMID: 11823416

Function and Biology Details

Reaction catalysed: 
Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form C1s (EC 3.4.21.42).
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133182 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Complement C1r subcomponent heavy chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 399 amino acids
Theoretical weight: 45.41 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P00736 (Residues: 307-705; Coverage: 58%)
Gene name: C1R
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC, MAN
Carbohydrate polymer
1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P212121
Unit cell:
a: 99.3Å b: 101.8Å c: 122.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.242 0.29
Expression system: Trichoplusia ni

Quick links

Citations

22 review citations

Complement System Part I - Molecular Mechanisms of Activation and Regulation.
Merle et al. (2015)
21 more

18 mentions without citation

Deciphering the fine details of c1 assembly and activation mechanisms: "mission impossible"?
Gaboriaud et al. (2014)
17 more