Linked Life Data

8223647

Source:http://linkedlifedata.com/resource/pubmed/id/8223647

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-12-22
pubmed:abstractText
We found that a seven-residue sequence in pro-adipokinetic hormone I (proAKH I) which precedes the endopeptidase cleavage site is predicted to form an omega loop. Molecular modelling experiments indicated that a stable omega loop may form at this site, and suggested that loop stability may depend on the C-terminal loop residue, Lys12. The importance of this residue in proAKH I processing was confirmed by the observation that replacement of Lys12 by thialysine, a Lys analog with an altered side chain, prevented processing in vivo. In addition we showed by molecular modelling that this side-chain alteration may prevent formation of an omega loop. Together, these approaches lead us to propose that an omega loop may serve as a recognition motif in proAKH I processing.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
217
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
905-11
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Structural requirements for processing of pro-adipokinetic hormone I.
pubmed:affiliation
Sussex Centre for Neuroscience, School of Biological Sciences, University of Sussex, Brighton, England.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't