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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1994-3-21
|
| pubmed:abstractText |
Newly-reported structural information about certain proximities between points on bound nucleotide and points on the heavy chain of myosin S-1 are incorporated into a previously-reported [Botts, J. Thomason, J.F. & Morales, M.F. Proc. Nat. Acad. Sci. USA, 86, 2204-2208 (1989)] structure of S-1. The resulting, enhanced structure is then used to identify some functionalities (e.g., the ATP-perturbable tryptophans), and to explain certain observations (e.g., some concerning the role of bound Mg2+ in the spectral response of TNBS-labelled Lys-83, and some concerning the response of the S-1 CD signal to nucleotide binding and to temperature change). These considerations lead to the suggestion that a strand of the 50 kDa "domain" (residues 510 to 540), and a strand of the 20 kDa 'domain' (residues 697-719) are involved in transmitting the effects of nucleotide binding and hydrolysis to the loop (constituted from the same "domain") that reaches a major (S-1)-actin interface.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0065-2598
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
332
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
235-40
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1993
|
| pubmed:articleTitle |
The region in myosin S-1 that may be involved in energy transduction.
|
| pubmed:affiliation |
Dept. of Physiology and Biophysics, University of the Pacific, San Francisco, CA 94115.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|