Isolation, sequence analysis, and biological activity of atrolysin E/D, the non-RGD disintegrin domain from Crotalus atrox venom

Archives of Biochemistry and Biophysics
K ShimokawaJ W Fox

Abstract

Crotalid snake venom metalloproteinases often have associated with them nonproteinase domains that may be processed from the mature proteinases. Nascent atrolysin E, from the western diamondback rattlesnake, Crotalus atrox, has a metalloproteinasedomain and a non-RGD disintegrin domain that is lacking in the mature metalloproteinase. In this studywe report on the isolation, sequence analysis, andbiological activity of the 7.4-kDa atrolysin E disintegrin domain (atrolysin E/D). Atrolysin E/D represents approximately 0.2% of the total protein fromthe crude venom. The protein begins with a glycinyl residue found in the latter part of the spacer region. The sequence of atrolysin E/D is identical to thatof the non-RGD disintegrin domain of atrolysin E. The structure is termed a non-RGD disintegrin sincein lieu of the characteristic RGD sequence, a Met-Val-Asp (MVD) is found instead. Nevertheless, the protein is a potent inhibitor of both collagen- and ADP-stimulated platelet aggregation with IC50 values of 4 and 8 nM, respectively. A cyclized synthetic peptide, Ac-CRVSMVDRNDDTC-NH2, which represents the sequence of the atrolysin E/D non-RGD loop, was demonstrated to be an effective inhibitor of platelet aggregation. Therefore, this ...Continue Reading

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Citations

Aug 10, 2000·Protein Science : a Publication of the Protein Society·J J CalveteJ W Fox
Jun 1, 2005·Toxicon : Official Journal of the International Society on Toxinology·Juan J CalveteLibia Sanz
Oct 27, 2018·Current Drug Targets·Pedro Henrique Souza CesarSilvana Marcussi
Apr 4, 2021·International Journal of Molecular Sciences·Danique L van den KerkhofIngrid Dijkgraaf
May 23, 2001·Archives of Biochemistry and Biophysics·D H SouzaH S Selistre-de-Araujo
Feb 1, 2011·Toxicon : Official Journal of the International Society on Toxinology·Tamara SajevicIgor Križaj

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