Literature DB >> 17485084

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

Tomoko Igarashi1, Satohiko Araki, Hidezo Mori, Soichi Takeda.   

Abstract

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.

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Year:  2007        PMID: 17485084     DOI: 10.1016/j.febslet.2007.04.057

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  29 in total

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Authors:  Linda Troeberg; Barbara Mulloy; Peter Ghosh; Meng-Huee Lee; Gillian Murphy; Hideaki Nagase
Journal:  Biochem J       Date:  2012-04-01       Impact factor: 3.857

2.  Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.

Authors:  Heli Liu; Ann H R Shim; Xiaolin He
Journal:  J Biol Chem       Date:  2009-08-18       Impact factor: 5.157

3.  Domain integration of ADAM family proteins: Emerging themes from structural studies.

Authors:  Tom Cm Seegar; Stephen C Blacklow
Journal:  Exp Biol Med (Maywood)       Date:  2019-07-23

4.  Molecular models of the Mojave rattlesnake (Crotalus scutulatus scutulatus) venom metalloproteinases reveal a structural basis for differences in hemorrhagic activities.

Authors:  Ruben K Dagda; Sardar E Gasanov; Boris Zhang; William Welch; Eppie D Rael
Journal:  J Biol Phys       Date:  2014-02-13       Impact factor: 1.365

Review 5.  ADAM proteases: ligand processing and modulation of the Notch pathway.

Authors:  A Zolkiewska
Journal:  Cell Mol Life Sci       Date:  2008-07       Impact factor: 9.261

Review 6.  A disintegrin and metalloproteinase-12 (ADAM12): function, roles in disease progression, and clinical implications.

Authors:  Erin K Nyren-Erickson; Justin M Jones; D K Srivastava; Sanku Mallik
Journal:  Biochim Biophys Acta       Date:  2013-05-13

7.  Systematic identification of barriers to human iPSC generation.

Authors:  Han Qin; Aaron Diaz; Laure Blouin; Robert Jan Lebbink; Weronika Patena; Priscilia Tanbun; Emily M LeProust; Michael T McManus; Jun S Song; Miguel Ramalho-Santos
Journal:  Cell       Date:  2014-07-17       Impact factor: 41.582

8.  The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.

Authors:  Linda Troeberg; Kazunari Fushimi; Simone D Scilabra; Hiroyuki Nakamura; Vincent Dive; Ida B Thøgersen; Jan J Enghild; Hideaki Nagase
Journal:  Matrix Biol       Date:  2009-07-28       Impact factor: 11.583

9.  Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2.

Authors:  Masamichi Nagae; Kousuke Yamanaka; Shinya Hanashima; Akemi Ikeda; Kana Morita-Matsumoto; Tadashi Satoh; Naoki Matsumoto; Kazuo Yamamoto; Yoshiki Yamaguchi
Journal:  J Biol Chem       Date:  2013-10-09       Impact factor: 5.157

10.  Structure of acostatin, a dimeric disintegrin from Southern copperhead (Agkistrodon contortrix contortrix), at 1.7 A resolution.

Authors:  Natalia Moiseeva; Robert Bau; Stephen D Swenson; Francis S Markland; Jun Yong Choe; Zhi Jie Liu; Marc Allaire
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2008-03-19
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