Near-planar solution structures of mannose-binding lectin oligomers provide insight on activation of lectin pathway of complement.

ABSTRACT: The complement system is a fundamental component of innate immunity that orchestrates complex immunological and inflammatory processes. Complement comprises over 30 proteins that eliminate invading microorganisms while maintaining host cell integrity. Protein-carbohydrate interactions play critical roles in both the activation and regulation of complement. Mannose-binding lectin (MBL) activates the lectin pathway of complement via the recognition of sugar arrays on pathogenic surfaces. To determine the solution structure of MBL, synchrotron x-ray scattering and analytical ultracentrifugation experiments showed that the carbohydrate-recognition domains in the MBL dimer, trimer, and tetramer are positioned close to each other in near-planar fan-like structures. These data were subjected to c

SUBMITTER: Miller A 

PROVIDER: S-EPMC3281675 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature