Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: evidence for signal, zymogen, and disintegrin-like structures - PubMed (original) (raw)
Comparative Study
. 1992 Jul 14;31(27):6203-11.
doi: 10.1021/bi00142a005.
Affiliations
- PMID: 1378300
- DOI: 10.1021/bi00142a005
Comparative Study
Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: evidence for signal, zymogen, and disintegrin-like structures
L A Hite et al. Biochemistry. 1992.
Abstract
The sequence of two overlapping cDNA clones for the zinc metalloproteinase hemorrhagic toxin e (also known as atrolysin e, EC 3.4.24.44) from the venom gland of Crotalus atrox, the Western diamondback rattlesnake, is presented. The assembled cDNA sequence is 1975 nucleotides in length and encodes an open reading frame of 478 amino acids. The mature hemorrhagic toxin e protein as isolated from the crude venom has a molecular weight of approximately 24,000 and thus represents the processed product of this open reading frame. From the deduced amino acid sequence, it can be hypothesized that the enzyme is translated with a signal sequence of 18 amino acids, an amino-terminal propeptide of 169 amino acids, a central hemorrhagic proteinase domain of 202 amino acids, and a carboxy-terminal sequence of 89 amino acids. The propeptide has a short region similar to the region involved in the activation of matrix metalloproteinase zymogens. The proteinase domain is similar to other snake venom metalloproteinases, with over 57% identity to the low molecular weight proteinases HR2a and H2-proteinase from the Habu snake Trimeresurus flavoviridis. The carboxy-terminal region, which is not observed in the mature protein, strongly resembles the protein sequence immediately following the proteinase domain of HR1B (a high molecular weight hemorrhagic proteinase from the venom of T. flavoviridis) and the members of a different family of snake venom polypeptides known for their platelet aggregation inhibitory activity, the disintegrins. The cDNA sequence bears striking similarity to a previously reported sequence for a disintegrin cDNA. This report is evidence that this subfamily of venom metalloproteinases is synthesized in a proenzyme form which must be proteolytically activated.(ABSTRACT TRUNCATED AT 250 WORDS)
Similar articles
- The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis.
Takeya H, Oda K, Miyata T, Omori-Satoh T, Iwanaga S. Takeya H, et al. J Biol Chem. 1990 Sep 25;265(27):16068-73. J Biol Chem. 1990. PMID: 2398046 - Molecular cloning of HR1a and HR1b, high molecular hemorrhagic factors, from Trimeresurus flavoviridis venom.
Kishimoto M, Takahashi T. Kishimoto M, et al. Toxicon. 2002 Sep;40(9):1369-75. doi: 10.1016/s0041-0101(02)00179-4. Toxicon. 2002. PMID: 12220724 - Biochemical characterization of atroxase and nucleotide sequence encoding the fibrinolytic enzyme.
TU AT, Baker B, Wongvibulsin S, Willis T. TU AT, et al. Toxicon. 1996 Nov-Dec;34(11-12):1295-300. doi: 10.1016/s0041-0101(96)00106-7. Toxicon. 1996. PMID: 9027985 Review. - Hemorrhagic metalloproteinases from snake venoms.
Bjarnason JB, Fox JW. Bjarnason JB, et al. Pharmacol Ther. 1994;62(3):325-72. doi: 10.1016/0163-7258(94)90049-3. Pharmacol Ther. 1994. PMID: 7972338 Review.
Cited by
- Snake Venom Metalloproteinases (SVMPs): A structure-function update.
Olaoba OT, Karina Dos Santos P, Selistre-de-Araujo HS, Ferreira de Souza DH. Olaoba OT, et al. Toxicon X. 2020 Jul 21;7:100052. doi: 10.1016/j.toxcx.2020.100052. eCollection 2020 Sep. Toxicon X. 2020. PMID: 32776002 Free PMC article. Review. - Toxinology provides multidirectional and multidimensional opportunities: A personal perspective.
Kini RM. Kini RM. Toxicon X. 2020 May 11;6:100039. doi: 10.1016/j.toxcx.2020.100039. eCollection 2020 Jun. Toxicon X. 2020. PMID: 32550594 Free PMC article. - Cell migration inhibition activity of a non-RGD disintegrin from Crotalus durissus collilineatus venom.
Oliveira IS, Manzini RV, Ferreira IG, Cardoso IA, Bordon KCF, Machado ART, Antunes LMG, Rosa JC, Arantes EC. Oliveira IS, et al. J Venom Anim Toxins Incl Trop Dis. 2018 Oct 20;24:28. doi: 10.1186/s40409-018-0167-6. eCollection 2018. J Venom Anim Toxins Incl Trop Dis. 2018. PMID: 30377432 Free PMC article. - Extracellular Matrix Remodeling in Human Disease.
Sonbol HS. Sonbol HS. J Microsc Ultrastruct. 2018 Jul-Sep;6(3):123-128. doi: 10.4103/JMAU.JMAU_4_18. J Microsc Ultrastruct. 2018. PMID: 30221137 Free PMC article. Review. - Structures and Functions of Snake Venom Metalloproteinases (SVMP) from Protobothrops venom Collected in Japan.
Oyama E, Takahashi H. Oyama E, et al. Molecules. 2017 Aug 4;22(8):1305. doi: 10.3390/molecules22081305. Molecules. 2017. PMID: 28777331 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources