Linked Life Data

14660664

Source:http://linkedlifedata.com/resource/pubmed/id/14660664

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2004-2-23
pubmed:databankReference
pubmed:abstractText
Dematin (band 4.9) is found in the junctional complex of the spectrin cytoskeleton that supports the erythrocyte cell membrane. Dematin is a member of the larger class of cytoskeleton-associated proteins that contain a modular "headpiece" domain at their extreme C termini. The dematin headpiece domain provides the second F-actin-binding site required for in vitro F-actin bundling. The dematin headpiece is found in two forms in the cell, one of 68 residues (DHP) and one containing a 22-amino acid insert near its N terminus (DHP+22). In addition, dematin contains the only headpiece domain that is phosphorylated, in vivo. The 22-amino acid insert in DHP+22 appeared unstructured in NMR spectra; therefore, we have determined the three-dimensional structure of DHP by multidimensional NMR methods. Although the overall three-dimensional structure of DHP is similar to that of the villin headpiece, there are two novel characteristics revealed by this structure. First, unlike villin headpiece that contains a single buried salt bridge, DHP contains a buried charged cluster comprising residues Glu(39), Arg(66), Lys(70), and the C-terminal carboxylate of Phe(76). Second, (15)N relaxation experiments indicate that the longer "variable loop" region near the N terminus of DHP (residues 20-29) is dynamic, undergoing significantly greater motions that the rest of the structure. Furthermore, NMR chemical shift changes indicate that the conformation of the dynamic variable loop is altered by phosphorylation of serine 74, which is far in the sequence from the variable loop region. Our results suggest that phosphorylation of the dematin headpiece acts as a conformational switch within this headpiece domain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7909-16
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:14660664-Actins, pubmed-meshheading:14660664-Amino Acid Sequence, pubmed-meshheading:14660664-Binding Sites, pubmed-meshheading:14660664-Blood Proteins, pubmed-meshheading:14660664-Carrier Proteins, pubmed-meshheading:14660664-Erythrocyte Membrane, pubmed-meshheading:14660664-Histidine, pubmed-meshheading:14660664-Humans, pubmed-meshheading:14660664-Magnetic Resonance Spectroscopy, pubmed-meshheading:14660664-Microfilament Proteins, pubmed-meshheading:14660664-Models, Molecular, pubmed-meshheading:14660664-Molecular Sequence Data, pubmed-meshheading:14660664-Molecular Structure, pubmed-meshheading:14660664-Peptide Fragments, pubmed-meshheading:14660664-Phosphoproteins, pubmed-meshheading:14660664-Phosphorylation, pubmed-meshheading:14660664-Protein Conformation, pubmed-meshheading:14660664-Serine
pubmed:year
2004
pubmed:articleTitle
The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site.
pubmed:affiliation
Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.