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. Author manuscript; available in PMC: 2014 Mar 15.
Published in final edited form as: Toxicon. 2013 Jan 10;64:43–54. doi: 10.1016/j.toxicon.2012.12.025

Fig. 2.

Fig. 2

Multiple alignment of predicted amino acid sequence of CamVMPII with other homologous venom proteins. The alignment was generated with the Clustal W multiple sequence alignment program with manual adjustment and displayed with box shaded. a) CamVMPII is closely homologous to class P-II snake venom metalloproteinases, metalloproteinase 2 (Met 2), CaVMP-II, agkistin, and jerdonitin. b) The disintegrin domain of CamVMPII (Cam-dis) is compared with other medium-sized disintegrins. The numbers in parenthesis are the NCBI accession numbers. The tripeptide binding motif are marked by the letter “X” above the sequences. All cysteine residues (letter “C” above the sequences) are conserved except for an extra cysteine residue (the letter “C” highlighted in black) in Cam-dis, salmosin 3, and albolatin.