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Structure paper

TitleThe structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions
Journal, issue, pagesJ. Mol. Biol., Vol. 342, Page 1533-1546, Year 2004
Publish dateAug 1, 2003 (structure data deposition date)
AuthorsHarmat, V. / Gal, P. / Kardos, J. / Szilagyi, K. / Ambrus, G. / Vegh, B. / Naray-Szabo, G. / Zavodsky, P.
External linksJ. Mol. Biol. / PubMed:15364579
MethodsX-ray diffraction
Resolution2.23 Å
Structure data

PDB-1q3x:
Crystal structure of the catalytic region of human MASP-2
Method: X-RAY DIFFRACTION / Resolution: 2.23 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / complement / serine protease / modular structure / hinge bending / autoactivation

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