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2DW2

Crystal structure of VAP2 from Crotalus atrox venom (Form 2-5 crystal)

Summary for 2DW2
Entry DOI10.2210/pdb2dw2/pdb
Related2DW0 2DW1
DescriptorCatrocollastatin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)][2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (5 entities in total)
Functional Keywordsapoptotic toxin, svmp, metalloproteinase, apoptosis, toxin
Biological sourceCrotalus atrox (western diamondback rattlesnake)
Total number of polymer chains2
Total formula weight97529.89
Authors
Takeda, S.,Igarashi, T.,Araki, S. (deposition date: 2006-08-02, release date: 2007-07-10, Last modification date: 2024-10-23)
Primary citationIgarashi, T.,Araki, S.,Mori, H.,Takeda, S.
Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins
Febs Lett., 581:2416-2422, 2007
Cited by
PubMed 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.
PubMed: 17485084
DOI: 10.1016/j.febslet.2007.04.057
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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