Linked Life Data

10591034

Source:http://linkedlifedata.com/resource/pubmed/id/10591034

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-2-17
pubmed:abstractText
Three bioactivity-variant neurotoxins, BmK M1, M4, and M8, have been purified from venom of the Chinese scorpion Buthus martensii Karsch. They possess distinct toxic activity on mice in vivo with different electrostatic properties. The relative toxicities of BmK M1, M4, and M8 are 13.3:2.5:1, which interestingly correspond to their respective pI values, ranging from basic to acidic, of 9.01, 7.53, and 5.30, respectively. In addition, the X-ray crystal structure of BmK M8, which is acidic and 1100 times less active than the most potent and basic alpha-toxin AaH II, have been determined at 1.85 A resolution and analyzed in detail. In combination with information from chemical modifications and site-directed mutagenesis, the structural comparisons and sequence alignments suggest a multisite binding mode for toxin-receptor interactions, and three "toxic regions" with relevance to the binding process, including Face A, Face B, and Site C. Face A is featured in the presence of several aromatic residues and may be more essential for the binding; Face B may contribute to the high efficacy of the binding process, on which substitution by acidic residues could weaken the toxic activity; Site C is probably involved in binding site specificity. The main residues involved in these regions will be discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1058-8108
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
309-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
A series of bioactivity-variant neurotoxins from scorpion Buthus martensii Karsch: X-ray crystal structure and functional implications.
pubmed:affiliation
Department of Protein Engineering, Chinese Academy of Sciences, Beijing, China.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't