› 1szb

X-ray diffraction
2.5Å resolution

Crystal structure of the human MBL-associated protein 19 (MAp19)

Released:
DOI: 10.2210/pdb1szb/pdb
PDB entry 1szb coloured by chain, front view.
PDB entry 1szb coloured by chain, side view.
PDB entry 1szb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin.
Gregory LA, Thielens NM, Matsushita M, Sorensen R, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C
J Biol Chem 279 29391-7 (2004)
PMID: 15117939

Function and Biology Details

Reaction catalysed: 
Selective cleavage after Arg(223) in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg(76) in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-126143 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannan-binding lectin serine protease 2 A chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 170 amino acids
Theoretical weight: 19.11 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: O00187 (Residues: 16-181; Coverage: 25%)
Gene name: MASP2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P43212
Unit cell:
a: 67.754Å b: 67.754Å c: 187.923Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.263 0.261 0.316
Expression system: Trichoplusia ni

Quick links

Citations

20 review citations

A journey through the lectin pathway of complement-MBL and beyond.
Garred et al. (2016)
19 more

4 mentions without citation

Analysis of nidogen-1/laminin γ1 interaction by cross-linking, mass spectrometry, and computational modeling reveals multiple binding modes.
Lössl et al. (2014)
3 more