Linked Life Data

10231520

Source:http://linkedlifedata.com/resource/pubmed/id/10231520

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1999-6-1
pubmed:databankReference
pubmed:abstractText
The mechanism by which the contractile machinery of muscle is assembled and maintained is not well-understood. Members of the cysteine-rich protein (CRP) family have been implicated in these processes. Three vertebrate CRPs (CRP1-3) that exhibit developmentally regulated muscle-specific expression have been identified. All three proteins are associated with the actin cytoskeleton, and one has been shown to be required for striated muscle structure and function. The vertebrate CRPs identified to date display a similar molecular architecture; each protein is comprised of two tandemly arrayed LIM domains, protein-binding motifs found in a number of proteins with roles in cell differentiation. Each LIM domain coordinates two Zn(II) ions that are bound independently in CCHC (C=Cys, H=His) and CCCC modules. Here we describe the solution structure of chicken CRP1 determined by homonuclear and 1H-15N heteronuclear magnetic resonance spectroscopy. Comparison of the structures of the two LIM domains of CRP1 reveals a high degree of similarity in their tertiary folds. In addition, the two component LIM domains represent two completely independent folding units and exhibit no apparent interactions with each other. The structural independence and spatial separation of the two LIM domains of CRP1 are compatible with an adapter or linker role for the protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5701-13
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10231520-Adaptor Proteins, Signal Transducing, pubmed-meshheading:10231520-Amino Acid Sequence, pubmed-meshheading:10231520-Animals, pubmed-meshheading:10231520-Avian Proteins, pubmed-meshheading:10231520-Carrier Proteins, pubmed-meshheading:10231520-Cell Differentiation, pubmed-meshheading:10231520-Chickens, pubmed-meshheading:10231520-Crystallography, X-Ray, pubmed-meshheading:10231520-LIM Domain Proteins, pubmed-meshheading:10231520-Models, Molecular, pubmed-meshheading:10231520-Molecular Sequence Data, pubmed-meshheading:10231520-Muscle, Smooth, pubmed-meshheading:10231520-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:10231520-Protein Structure, Secondary, pubmed-meshheading:10231520-Protein Structure, Tertiary, pubmed-meshheading:10231520-Solutions, pubmed-meshheading:10231520-Zinc Fingers
pubmed:year
1999
pubmed:articleTitle
Solution structure of the chicken cysteine-rich protein, CRP1, a double-LIM protein implicated in muscle differentiation.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Maryland Baltimore County 21250, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't