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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
21
|
| pubmed:dateCreated |
1998-6-12
|
| pubmed:databankReference | |
| pubmed:abstractText |
Tropomyosins (TMs) are highly conserved, coiled-coil, actin binding regulatory proteins found in most eukaryotic cells. The amino-terminal domain of 284-residue TMs is among the most conserved and functionally important regions. The first nine residues are proposed to bind to the carboxyl-terminal nine residues to form the "overlap" region between successive TMs, which bind along the actin filament. Here, the structure of the N-terminus of muscle alpha-TM, in a chimeric peptide, TMZip, has been solved using circular dichroism (CD) and two-dimensional proton nuclear magnetic resonance (2D 1H NMR) spectroscopy. Residues 1-14 of TMZip are the first 14 N-terminal residues of rabbit striated alpha-TM, and residues 15-32 of TMZip are the last 18 C-terminal residues of the yeast GCN4 transcription factor. CD measurements show that TMZip forms a two-stranded coiled-coil alpha-helix with an enthalpy of folding of -34 +/- 2 kcal/mol. In 2D1H NMR studies at 15 degrees C, pH 6.4, the peptide exhibits 123 sequential and medium range intrachain NOE cross peaks per chain, characteristic of alpha-helices extending from residue 1 to residue 29, together with 85 long-range NOE cross peaks arising from interchain interactions. The three-dimensional structure of TMZip has been determined using these data plus an additional 509 intrachain constraints per chain. The coiled-coil domain extends to the N-terminus. Amide hydrogen exchange studies, however, suggest that the TM region is less stable than the GCN4 region. The work reported here is the first atomic-resolution structure of any region of TM and it allows insight into the mechanism of the function of the highly conserved N-terminal domain.
|
| 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 |
26
|
| pubmed:volume |
37
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
7834-43
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:9601044-Amino Acid Sequence,
pubmed-meshheading:9601044-Animals,
pubmed-meshheading:9601044-Crystallography, X-Ray,
pubmed-meshheading:9601044-Leucine Zippers,
pubmed-meshheading:9601044-Molecular Sequence Data,
pubmed-meshheading:9601044-Muscle, Skeletal,
pubmed-meshheading:9601044-Muscle Proteins,
pubmed-meshheading:9601044-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9601044-Peptides,
pubmed-meshheading:9601044-Protein Engineering,
pubmed-meshheading:9601044-Protein Folding,
pubmed-meshheading:9601044-Protein Structure, Secondary,
pubmed-meshheading:9601044-Rabbits,
pubmed-meshheading:9601044-Recombinant Fusion Proteins,
pubmed-meshheading:9601044-Saccharomyces cerevisiae,
pubmed-meshheading:9601044-Sequence Homology, Amino Acid,
pubmed-meshheading:9601044-Tropomyosin
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
The structure of the N-terminus of striated muscle alpha-tropomyosin in a chimeric peptide: nuclear magnetic resonance structure and circular dichroism studies.
|
| pubmed:affiliation |
Department of Neuroscience and Cell Biology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854-5635, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|