2jhh

From Proteopedia

Revision as of 15:47, 30 October 2007

STRUCTURE OF GLOBULAR HEADS OF M-FICOLIN AT ACIDIC PH

Overview

Ficolins are soluble oligomeric proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition, domains. They act as innate immune sensors by recognizing conserved, molecular markers exposed on microbial surfaces and thereby triggering, effector mechanisms such as enhanced phagocytosis and inflammation. In, humans, L- and H-ficolins have been characterized in plasma, whereas a, third species, M-ficolin, is secreted by monocytes and macrophages. To, decipher the molecular mechanisms underlying their recognition properties, we previously solved the structures of the recognition domains of L- and, H-ficolins, in complex with various model ligands (Garlatti et al. (2007), EMBO J. 24: 623-633). We now report the ligand-bound crystal structures of, ... [(full description)]

About this Structure

2JHH is a [Single protein] structure of sequence from [Homo sapiens] with CA as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch., Garlatti V, Martin L, Gout E, Reiser JB, Fujita T, Arlaud GJ, Thielens NM, Gaboriaud C, J Biol Chem. 2007 Sep 26;. PMID:17897951

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