3POB
Crystal structure of MASP-1 CUB2 domain in complex with the collagen-like domain of MBL
Summary for 3POB
Entry DOI | 10.2210/pdb3pob/pdb |
Descriptor | Mannan-binding lectin serine protease 1, MBL collagen-like peptide, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | collagen complex, masp, cub domain, mbl, mbp, collagen peptide, calcium binding site, complement proteins, lectin pathway of complement, masp-1, bloodstream, hydrolase |
Biological source | Rattus norvegicus (brown rat,rat,rats) More |
Cellular location | Secreted: Q8CHN8 |
Total number of polymer chains | 4 |
Total formula weight | 20570.69 |
Authors | Gingras, A.R.,Moody, P.C.E.,Wallis, R. (deposition date: 2010-11-22, release date: 2011-08-24, Last modification date: 2023-09-06) |
Primary citation | Gingras, A.R.,Girija, U.V.,Keeble, A.H.,Panchal, R.,Mitchell, D.A.,Moody, P.C.,Wallis, R. Structural Basis of Mannan-Binding Lectin Recognition by Its Associated Serine Protease MASP-1: Implications for Complement Activation. Structure, 19:1635-1643, 2011 Cited by PubMed Abstract: Complement activation contributes directly to health and disease. It neutralizes pathogens and stimulates immune processes. Defects lead to immunodeficiency and autoimmune diseases, whereas inappropriate activation causes self-damage. In the lectin and classical pathways, complement is triggered upon recognition of a pathogen by an activating complex. Here we present the first structure of such a complex in the form of the collagen-like domain of mannan-binding lectin (MBL) and the binding domain of its associated protease (MASP-1/-3). The collagen binds within a groove using a pivotal lysine side chain that interacts with Ca(2+)-coordinating residues, revealing the essential role of Ca(2+). This mode of binding is prototypic for all activating complexes of the lectin and classical pathways, and suggests a general mechanism for the global changes that drive activation. The structural insights reveal a new focus for inhibitors and we have validated this concept by targeting the binding pocket of the MASP. PubMed: 22078562DOI: 10.1016/j.str.2011.08.014 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.801 Å) |
Structure validation
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