Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 64, Issue -, Pages 781-784Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S174430910802294X
Keywords
-
Funding
- European Community
- Hungarian National Office for Research and Technology (NKTH) [NKFP_07_1-MASPOK07]
- Hungarian Scientific Research Fund (OTKA) [NI61915, F67937, NK67800]
- [RII3-CT-2004-506008]
Ask authors/readers for more resources
MASP-1, a multidomain serine protease, is a component of the lectin pathway of complement. Its precise function is unknown, although it seems to enhance the complement-activating capacity of MASP-2, a related enzyme. MASP-1 has also been implicated as playing a role in blood coagulation. It is mostly found associated with mannose-binding lectin (MBL) and ficolins. Early attempts to crystallize MASP-1 failed because of the inhomogeneity of the purified material. MASP-1 was shown by acidic nondenaturing PAGE to be composed of differently charged species, which are most likely to be the products of deamidation occurring during the refolding procedure. Sequential cation-exchange and anion-exchange chromatography resulted in a homogeneous material, which was successfully crystallized. The best crystal diffracted to 2.55 angstrom resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.4, b = 70.4, c = 121.4 angstrom. The crystal structure of MASP-1 may help in understanding the function of this mysterious serine protease.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available