On the ancestral recruitment of metalloproteinases into the venom of snakes.

Authors :: Casewell NR
Source :: Toxicon : official journal of the International Society on Toxinology [Toxicon] 2012 Sep 15; Vol. 60 (4), pp. 449-54. Date of Electronic Publication: 2012 Mar 03.
Publication Year :: 2012
Abstract: Tracing the evolutionary history of proteins can reveal insights into gene alterations responsible for changes in structure and function. Here, the origin of snake venom metalloproteinases was rigorously reassessed using phylogenetics and the reconstruction of ancestral sequences. Basal SVMPs are most closely related to ADAM 7, 28 and decysin-1 proteins. Reconstructing the evolutionary history of these proteins and their hypothetical ancestors reveals progressive alterations in the amino acid composition and structural characteristics of ADAMs/SVMPs through evolutionary time.<br /> (Copyright © 2012 Elsevier Ltd. All rights reserved.)

Subjects :: ADAM Proteins chemistry
ADAM Proteins genetics
ADAM Proteins metabolism
Amino Acid Sequence
Animals
Humans
Metalloendopeptidases chemistry
Metalloendopeptidases genetics
Metalloendopeptidases metabolism
Metalloproteases chemistry
Metalloproteases genetics
Molecular Sequence Data
Phylogeny
Snake Venoms chemistry
Snake Venoms genetics
Evolution, Molecular
Metalloproteases metabolism
Snake Venoms enzymology

Language :: English
ISSN :: 1879-3150
Volume :: 60
Issue :: 4
Database :: MEDLINE
Journal :: Toxicon : official journal of the International Society on Toxinology
Publication Type :: Academic Journal
Accession number :: 22406471
Full Text :: https://doi.org/10.1016/j.toxicon.2012.02.006