The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Conformational transition accompanying the binding of calcium(2+) ion to the protein activator of 3',5'-cyclic adenosine monophosphate phosphodiesterase
Abstract
The Ca2+-dependent protein activator of 3':5'-cyclic adenosine monophosphate phosphodiesterase is shown to undergo a conformational transition upon binding of 2 mol of Ca2+/mol of activator. Circular dichroic studies indicate that Ca2+ induces an increase of 5-8% in alpha-helix content with a concomitant decrease in the amount of random coil. In the absence of Ca2+ and in the presence of [ethylenebis(oxoethylenenitrilo)]tetraacetic acid (EGTA), the protein contains 30-35% alpha helix, 50% random coil, and 15-20% beta-pleated sheat. Spectrophotometric titration indicates that the two tyrosyl residues have pK's of 10.4 and 11.9 and are therefore in different environments. The Ca2+-induced conformational change is accompanied by an increased exposure to protons of the partially exposed tyrosine, as shown by a shift in its pK from 10.4 to 10.). Increased solvation is also consistent with a negative difference spectrum at 287 and 279 nm as seen upon Ca2+ binding. Modification in the environment of all or some of the phenylalanine residues also is part of the conformational change accompanying Ca2+ binding. A new and rapid purification procedure which yields large amounts (25-30% yields) of homogenous protein activator and a direct and sensitive assay procedure for cAMP phosphodiesterase and its activator are also described.
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Citations
Cites
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Cited by
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Metadata
- Authors
- Klee, C. B.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1977-03-08
- Volume
- 16
- Issue
- 5
- Pages
- 1017-1024
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2002204004
- Cited by
- 472
- References
- 23
- FWCI
- 13.40
- Type
- journal article
- Language
- en
- Open access
- closed
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