<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>169(3)</volume><submitter>Guan HH</submitter><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 </pubmed_abstract><journal>Journal of structural biology</journal><pagination>294-303</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7129284</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins.</pubmed_title><pmcid>PMC7129284</pmcid><pubmed_authors>Huang YW</pubmed_authors><pubmed_authors>Wu PL</pubmed_authors><pubmed_authors>Chen CJ</pubmed_authors><pubmed_authors>Jeyakanthan J</pubmed_authors><pubmed_authors>Goh KS</pubmed_authors><pubmed_authors>Davamani F</pubmed_authors><pubmed_authors>Wu WG</pubmed_authors><pubmed_authors>Guan HH</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins.</name><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 </description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Mar</publication><modification>2026-05-03T07:32:13.874Z</modification><creation>2026-04-07T18:56:41.178Z</creation></dates><accession>S-EPMC7129284</accession><cross_references><pubmed>19932752</pubmed><doi>10.1016/j.jsb.2009.11.009</doi></cross_references></HashMap>