{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["169(3)"],"submitter":["Guan HH"],"pubmed_abstract":["The structures of snake venom metalloproteases (SVMPs) are proposed to be useful models to understand the structural and functional relationship of ADAM (a disintegrin and metalloprotease) which are membrane-anchored proteins involved in multiple human diseases. We have purified, sequenced and determined the structures of two new P-III SVMPs - atragin and kaouthiagin-like (K-like) from Naja atra. Atragin exhibits a known C-shaped topology, whereas K-like adopts an I-shaped conformation because of the distinct disulfide pattern in the disintegrin-like (D) domain. K-like exhibits an enzymatic specificity toward pro-TNFalpha with less inhibition of cell migration, but atragin shows the opposite effect. The specificity of the enzymatic activity is indicated to be dominated mainly by the local "],"journal":["Journal of structural biology"],"pagination":["294-303"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7129284"],"repository":["biostudies-literature"],"pubmed_title":["Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins."],"pmcid":["PMC7129284"],"pubmed_authors":["Huang YW","Wu PL","Chen CJ","Jeyakanthan J","Goh KS","Davamani F","Wu WG","Guan HH"],"additional_accession":[]},"is_claimable":false,"name":"Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins.","description":"The structures of snake venom metalloproteases (SVMPs) are proposed to be useful models to understand the structural and functional relationship of ADAM (a disintegrin and metalloprotease) which are membrane-anchored proteins involved in multiple human diseases. We have purified, sequenced and determined the structures of two new P-III SVMPs - atragin and kaouthiagin-like (K-like) from Naja atra. Atragin exhibits a known C-shaped topology, whereas K-like adopts an I-shaped conformation because of the distinct disulfide pattern in the disintegrin-like (D) domain. K-like exhibits an enzymatic specificity toward pro-TNFalpha with less inhibition of cell migration, but atragin shows the opposite effect. The specificity of the enzymatic activity is indicated to be dominated mainly by the local ","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Mar","modification":"2026-05-03T07:32:13.874Z","creation":"2026-04-07T18:56:41.178Z"},"accession":"S-EPMC7129284","cross_references":{"pubmed":["19932752"],"doi":["10.1016/j.jsb.2009.11.009"]}}