Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor

Kini, R. Manjunatha; Evans, Herbert J.

doi:10.1016/0041-0101(92)90869-7

Cited by 222 publications

(111 citation statements)

References 108 publications

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“…These peptidases include the astacins [9-131, the snake venom zinc endopeptidases [14,15] [12,13,16]. These structures reveal that both proteinases exhibit (in spite of low overall sequence similarity) significant topological equivalence and especially a virtually identical zinc environment, including a common 'Met-turn'.…”

Section: Introductionmentioning

confidence: 99%

Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’

1993

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The X-ray crystal structures of two zmc endopeptldases. astacin from crayfish. and adamalysm II from snake venom, reveal a strong overall lopologlcal equivalence and virtually Identical extended HEXXHXXGXXH zinc-binding segments, but m addition a methlomne-containing turn of similar conformatlon (the 'Met-turn'). which forms a hydrophobic basis for the zmc ion and the three ligandmg hlstidine residues. These two features are also present in a similar arrangement m the matrix metalloproteinases (matrixins) and in the large bacterial Serratra proteinase-like peptidases (serralysins).We suggest that these four proteinases represent members of distinct subfamilies which can be grouped together in a family, for which we propose the designation, metzmcins.Astacm; Snake venom metalloproteinase; Matrix metalloprotemase; Thermolysm; Zmc endopeptidase family: Protein crystal structure

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Section: Introductionmentioning

confidence: 99%

Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’

1993

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“…To date over a hundreds SVMPs have been reported, and classified into the following four classes according to the domain structure/molecular size: P-I, composed of only metalloproteinase domain/20-30 kDa; P-II, containing metalloproteinase and disintegrin domains/30-50 kDa; P-III, consisting of metalloproteinase, disintegrin-like and Cys-rich/50-80 kDa; and P-IV, containing an additional C-type lectin sequence at the C-terminal of P-III/80-100 kDa (Hite et al, 1994;Kini and Evans, 1992). All the metalloproteinases have zinc-binding sites (HExGHxxGxxH), and cysteine residue in prodomain chelates to zinc in the latent form.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

et al. 2006

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-During the characterization of hemorrhagic factor in venom of Rhabdophis tigrinus tigrinus, so-called Yamakagashi in Japan, one of the Colubridae family, a novel metalloproteinase with molecular weight of 38 kDa in the Duvernoy's gland of Yamakagashi was identified by gelatin zymography and by monitoring its proteolytic activity using a fluorescence peptide substrate, MOCAc-PLGLA 2 pr(Dnp)AR-NH 2 , which was developed for measuring the well-known matrix metalloproteinase (MMP) activity.After purification by gel filtration HPLC and/or column switch HPLC system consisting of an affinity column, which was immobilized with a synthetic BS-10 peptide (MQKPRCGVPD) originating from propeptide domain of MMP-7 and a reversed-phase column, the N-terminal amino acid sequence of the 38 kDa metalloproteinase was identified as FNTFPGDLK which shared a high homology to Xenopus MMP-9.The 38 kDa metalloproteinase required Zn 2+ and Ca 2+ ions for its proteolytic activity. In addition, the proteolytic activity was almost completely inhibited by BS-10, a MMP inhibitor, but not by the serine proteinase inhibitors, cysteine proteinase inhibitors and aspartic proteinase inhibitors.Together these results demonstrated that the 38 kDa proteinase is a novel snake verom metalloproteinase (SVMP) containing HExGHxxGxxH motif which possesses high affinity to the BS-10 peptide, into its molecule, and the enzymatic properties are closed to that of MMPs.Based on the results obtained in the present study, we concluded that the 38 kDa metalloproteinase is a novel metalloproteinase whose activity may be regulated by the cysteine switch mechanism, and could be classified as one of the matrix metalloproteinases rather than snake venom metalloproteinases.

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“…In their venom glands, snakes of the family Crotalidae (adders) produce extremely aggressive proteolytic enzymes, which can cause hemorrhage and tissue necrosis (see reviews by Bjarnason Takeya et al, 1990;Hite et al, 1992Hite et al, , 1994Kini & Evans, 1992). These toxins have been named adamalysins after adamalysin 11, an enzyme from the rattlesnake Crotalus adamanteus (Gomis-Ruth et al, 1993a.…”

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confidence: 99%

The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

et al. 1995

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The three-dimensional structures of the zinc endopeptidases human neutrophil collagenase, adamalysin I1 from rattle snake venom, alkaline proteinase from Pseudomonas aeruginosa, and astacin from crayfish are topologically similar, with respect to a five-stranded 0-sheet and three a-helices arranged in typical sequential order. The four proteins exhibit the characteristic consensus motif HEXXHXXGXXH, whose three histidine residues are involved in binding of the catalytically essential zinc ion. Moreover, they all share a conserved methionine residue beneath the active site metal as part of a superimposable "Met-turn.'' This structural relationship is supported by a sequence alignment performed on the basis of topological equivalence showing faint but distinct sequential similarity. The alkaline proteinase is about equally distant (26% sequence identity) to both human neutrophil collagenase and astacin and a little further away from adamalysin I1 (17% identity). The pairs astacin/adamalysin 11, astacidhuman neutrophil collagenase, and adamalysin Whuman neutrophil collagenase exhibit sequence identities of 16%, 14%, and 13%, respectively. Therefore, the corresponding four distinct families of zinc peptidases, the astacins, the matrix metalloproteinases (matrixins, collagenases), the adamalysins/reprolysins (snake venom proteinases/reproductive tract proteins), and the serralysins (large bacterial proteases from Serratia, Erwinia, and Pseudomonas) appear to have originated by divergent evolution from a common ancestor and form a superfamily of proteolytic enzymes for which the designation "metzincins" has been proposed. There is also a faint but significant structural relationship of the metzincins to the thermolysin-like enzymes, which share the truncated zincbinding motif HEXXH and, moreover, similar topologies in their N-terminal domains.Keywords: crystal structure; metalloproteinase; molecular evolution; protein family; sequence alignment; topology is involved in metal binding (McKerrow, 1987;

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Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor

Cited by 222 publications

References 108 publications

Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’

Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

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