About: Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins

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About: Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins
Creator	Chen, Chun-Jung Davamani, Fabian Goh, King-Siang Guan, Hong-Hsiang Huang, Yen-Wei Jeyakanthan, Jeyaraman Wu, Po-Long Wu, Wen-Guey
Source	Elsevier; Medline; PMC
abstract	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-TNFα 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 structures of SVMP in the metalloprotease (M) domain, whereas the hyper-variable region (HVR) in the cysteine-rich (C) domain is involved in a cell-migration activity. We demonstrate also a pH-dependent enzymatic activity of atragin that we correlate with the structural dynamics of a Zn2+-binding motif and the Met-turn based on the structures determined with a pH-jump method. The structural variations between the C- and I-shapes highlight the disulfide bond patterns in the D domain of the ADAM/adamalysin/reprolysins family proteins.
has issue date	2010-03-31(xsd:dateTime)
bibo:doi	10.1016/j.jsb.2009.11.009
bibo:pmid	19932752
has license	els-covid
sha1sum (hex)	7a6e1e716a2b9327e8c21f8b6ba6a07736e6c085
schema:url	https://doi.org/10.1016/j.jsb.2009.11.009
resource representing a document's title	Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins
has PubMed Central identifier	PMC7129284
has PubMed identifier	19932752
schema:publication	Journal of Structural Biology
resource representing a document's body	covid:7a6e1e716a2b9327e8c21f8b6ba6a07736e6c085#body_text
is schema:about of	named entity 'FAMILY' named entity 'cell migration' named entity 'structures' named entity 'enzymatic' named entity 'SPECIFICITY' named entity 'LOCAL' named entity 'PH-' named entity 'TNFA' named entity 'FAMILY' named entity 'MET-' named entity 'STRUCTURES' named entity 'ADAM' named entity 'MEMBRANE' named entity 'MIGRATION' named entity 'DYNAMICS' named entity 'PRO-' named entity 'PURIFIED' named entity 'OPPOSITE' named entity 'UNDERSTAND' named entity 'MULTIPLE' named entity 'DISULFIDE' named entity 'ADAMALYSIN' named entity 'NAJA ATRA' named entity 'DOMAIN' named entity 'EXHIBITS' named entity 'KAOUTHIAGIN' named entity '28A' named entity 'SHAPED' named entity 'RICH' named entity 'MOTIF' named entity 'PATTERNS' named entity 'CYSTEINE' named entity 'PATTERN' named entity 'DISULFIDE BOND' named entity 'EFFECT' named entity 'NEW' named entity 'METHOD' named entity 'SNAKE VENOM' named entity 'DISULFIDE' named entity 'MODELS' named entity 'PROTEINS' named entity 'ACTIVITY' named entity 'DEPENDENT' named entity 'ENZYMATIC' named entity 'ANCHORED' named entity 'HUMAN DISEASES' named entity 'METALLOPROTEASE' named entity 'SNAKE VENOM' named entity 'VARIATIONS' named entity 'TURN' named entity 'STRUCTURAL' named entity 'VARIABLE REGION' named entity 'BINDING' named entity 'A CELL' named entity 'DISTINCT' named entity 'LIKE' named entity 'III' named entity 'PATTERNS' named entity 'STRUCTURES' named entity 'DOMAIN' named entity 'DETERMINED' named entity 'HAVE' named entity 'METALLOPROTEASES' named entity 'CONFORMATION' named entity 'USEFUL' named entity 'PROPOSED' named entity 'BASED' named entity 'SHAPES' named entity 'JUMP' named entity 'INVOLVED' named entity 'ENZYMATIC ACTIVITY' named entity 'KNOWN' named entity 'TOPOLOGY' named entity 'BUT'

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