The Library
Structural Basis of Mannan-Binding Lectin Recognition by Its Associated Serine Protease MASP-1: Implications for Complement Activation
Tools
Tools
Tools
Gingras, Alexandre R., Girija, Umakhanth Venkatraman, Keeble, Anthony H., Panchal, Roshni, Mitchell, Daniel A., Moody, Peter C. E. and Wallis, Russell (2011) Structural Basis of Mannan-Binding Lectin Recognition by Its Associated Serine Protease MASP-1: Implications for Complement Activation. Structure, Vol.19 (No.11). pp. 1635-1643. doi:10.1016/j.str.2011.08.014 ISSN 0969-2126.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Official URL: http://dx.doi.org/10.1016/j.str.2011.08.014
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.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | R Medicine > R Medicine (General) | ||||
| Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School | ||||
| Journal or Publication Title: | Structure | ||||
| Publisher: | Cell Press | ||||
| ISSN: | 0969-2126 | ||||
| Official Date: | 2011 | ||||
| Dates: |
|
||||
| Volume: | Vol.19 | ||||
| Number: | No.11 | ||||
| Number of Pages: | 9 | ||||
| Page Range: | pp. 1635-1643 | ||||
| DOI: | 10.1016/j.str.2011.08.014 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
