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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2001-1-2
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pubmed:abstractText |
The cysteine-rich proteins (CRPs) are a family of highly conserved LIM (an acronym derived from the three gene products lin-11, isl-1 and mec-3) domain proteins that have been implicated in muscle differentiation. All CRP family members characterized so far have been shown to interact with the filamentous actin cross-linker alpha-actinin. The region of CRP required for this interaction has previously been broadly mapped to the molecule's N-terminal half. Here we report that the alpha-actinin-binding region of CRP, which we have mapped by using a combination of blot overlay and Western immunoblot techniques, is confined to an 18-residue sequence occurring within the protein's N-terminal glycine-rich repeat. A site-directed mutagenesis analysis of the binding region has revealed the critical importance of a single lysine residue (lysine 65 in human CRP1). Alterations at this site lead to a 10-fold decrease in alpha-actinin binding in comparison with wild-type CRP. The critical lysine residue localizes within a short alpha-helix, raising the possibility that mutagenesis-induced alterations in alpha-actinin-binding capacity might be attributed to the disruption of a key structural element.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-10090149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-10231520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-10397768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-1374386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-1469049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-1541635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-1734023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-2112549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-7938009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-7954790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-7954791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-8294495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-8361751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-8662982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-8663233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-8794860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-8922390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9039266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9129143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9281590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9314536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9341203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9394617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9560318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9594664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9722554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10926853-9815145
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
350 Pt 1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
269-74
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10926853-Actinin,
pubmed-meshheading:10926853-Amino Acid Sequence,
pubmed-meshheading:10926853-Binding Sites,
pubmed-meshheading:10926853-Cysteine,
pubmed-meshheading:10926853-Glycine,
pubmed-meshheading:10926853-LIM Domain Proteins,
pubmed-meshheading:10926853-Molecular Sequence Data,
pubmed-meshheading:10926853-Muscle Proteins,
pubmed-meshheading:10926853-Nuclear Proteins,
pubmed-meshheading:10926853-Protein Conformation,
pubmed-meshheading:10926853-Sequence Homology, Amino Acid
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pubmed:year |
2000
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pubmed:articleTitle |
Fine mapping of the alpha-actinin binding site within cysteine-rich protein.
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pubmed:affiliation |
Department of Biology and Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84112-5550, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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