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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
22
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pubmed:dateCreated |
1993-7-8
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pubmed:abstractText |
The purine binding site of ATP on skeletal muscle myosin has been photoaffinity labeled with 2-azidoadenosine diphosphate (2-N3ADP). 2-N3ADP was stably trapped at the active site (t1/2 approximately 5 days, 0 degree C) by complexation of the two heavy chain reactive thiols (Cys-697 and Cys-707) with Co(III)phenanthroline. Photoincorporation occurred only in the 23-kDa NH2-terminal tryptic fragment of the heavy chain. Extensive serial digestion of photolabeled subfragment 1 of myosin by trypsin and subtilisin yielded a series of labeled peptides which were purified by HPLC. Sequence and radiolabeling analysis of eight photolabeled peptides all indicated that tryptophan-130 was the only labeled residue. This site of labeling confirms earlier photolabeling studies with the non-nucleotide ADP analogue, 2[(4-azido-2-nitrophenyl)-amino]ethyl diphosphate (NANDP), which also labeled Trp-130 [Okamoto, Y., & Yount, R. G. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 1575-1579]. Comparison of the structures of 2-N3ADP and NANDP indicate that their azido groups can be superimposed if both analogues bind to the active site in an extended conformation in a manner analogous to the anti conformation of ATP.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-azidoadenosine 5'-triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Azides,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Subfragments,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5725-32
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8504091-Adenosine Triphosphate,
pubmed-meshheading:8504091-Affinity Labels,
pubmed-meshheading:8504091-Amino Acid Sequence,
pubmed-meshheading:8504091-Animals,
pubmed-meshheading:8504091-Azides,
pubmed-meshheading:8504091-Binding Sites,
pubmed-meshheading:8504091-Chromatography, High Pressure Liquid,
pubmed-meshheading:8504091-Molecular Conformation,
pubmed-meshheading:8504091-Molecular Sequence Data,
pubmed-meshheading:8504091-Muscles,
pubmed-meshheading:8504091-Myosin Subfragments,
pubmed-meshheading:8504091-Myosins,
pubmed-meshheading:8504091-Peptide Fragments,
pubmed-meshheading:8504091-Photochemistry,
pubmed-meshheading:8504091-Rabbits,
pubmed-meshheading:8504091-Sequence Analysis,
pubmed-meshheading:8504091-Trypsin
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pubmed:year |
1993
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pubmed:articleTitle |
Photoaffinity labeling of skeletal myosin with 2-azidoadenosine triphosphate.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.
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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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