Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins | Zendy

Igarashi Tomoko | Zendy; Araki Satohiko | Zendy; Mori Hidezo | Zendy; Takeda Soichi | Zendy

Premium

Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins

Author(s) -

Igarashi Tomoko,

Araki Satohiko,

Mori Hidezo,

Takeda Soichi

Publication year - 2007

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2007.04.057

Subject(s) - disintegrin , venom , metalloproteinase , monomer , crystal structure , protein family , cysteine , chemistry , stereochemistry , microbiology and biotechnology , biology , biochemistry , matrix metalloproteinase , crystallography , enzyme , gene , organic chemistry , polymer

Catrocollastatin/vascular apoptosis‐inducing protein (VAP)2B is a metalloproteinase from Crotalus atrox venom, possessing metalloproteinase/disintegrin/cysteine‐rich (MDC) domains that bear the typical domain architecture of a disintegrin and metalloproteinase (ADAM)/adamalysin/reprolysin family proteins. Here we describe crystal structures of catrocollastatin/VAP2B in three different crystal forms, representing the first reported crystal structures of a member of the monomeric class of this family of proteins. The overall structures show good agreement with both monomers of atypical homodimeric VAP1. Comparison of the six catrocollastatin/VAP2B monomer structures and the structures of VAP1 reveals a dynamic, modular architecture that may be important for the functions of ADAM/adamalysin/reprolysin family proteins.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research