New binding face of C-type lectin-like domains

Hideo Fukuhara; Atsushi Furukawa; Katsumi Maenaka

doi:10.1016/j.str.2014.11.001

New binding face of C-type lectin-like domains

Structure. 2014 Dec 2;22(12):1694-1696. doi: 10.1016/j.str.2014.11.001.

Authors

Hideo Fukuhara¹, Atsushi Furukawa¹, Katsumi Maenaka²

Affiliations

¹ Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
² Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; CREST, Japan Science and Technology Agency, Saitama 332-0012, Japan. Electronic address: maenaka@pharm.hokudai.ac.jp.

PMID: 25470427
DOI: 10.1016/j.str.2014.11.001

Abstract

C-type lectin-like receptor 2 (CLEC-2) is a member of the C-type lectin (like) receptor (CLR) family that uses a Ca(2+) binding domain to bind specific glycans. However, in this issue of Structure, Nagae and colleagues report on how the structures of CLEC-2 in complex with a glycopeptide podoplanin and a snake venom protein, rhodocytin, show a different mode of binding.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Lectins, C-Type / metabolism*
Membrane Glycoproteins / metabolism*
Models, Molecular*
Viper Venoms / metabolism*

Substances

Lectins, C-Type
Membrane Glycoproteins
Viper Venoms