Linked Life Data

7727365

Source:http://linkedlifedata.com/resource/pubmed/id/7727365

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
37
pubmed:dateCreated
1995-5-30
pubmed:abstractText
A crustacean-specific toxin from the Mexican scorpion Centruroides limpidus limpidus was purified, and its primary sequence was determined, including disulfide bonds. This toxin has 66 amino acid residues and is stabilized by four disulfide bridges (Cys12-Cys65, Cys16-Cys41, Cys25-Cys46, and Cys29-Cys48). A detailed nuclear magnetic resonance structure of this protein was obtained using a combination of two-dimensional proton NMR experiments. The NMR parameters that gave 69 dihedral restraints and 418 distance constraints were used in molecular dynamics calculations in order to determine the solution conformation of the toxin. It is composed of a short alpha-helix and a three-stranded antiparallel beta-sheet. Although the regular secondary structure of this crustacean toxin is common to the structural motif of other scorpion toxins, detailed conformational analysis was performed in order to highlight structural features that might be responsible for the differential modulation of the toxin on sodium channels of distinct tissues: mammalian versus crustacean.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11135-49
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Primary and NMR three-dimensional structure determination of a novel crustacean toxin from the venom of the scorpion Centruroides limpidus limpidus Karsch.
pubmed:affiliation
Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't