The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Space-Filling Models of Kinase Clefts and Conformation Changes: Comparison of the surface structures of kinase enzymes implicates closing clefts in their mechanism.
Abstract
Space-filling models of yeast hexokinase, adenylate kinase, and phosphoglycerate kinase drawn by computer clearly portray the bilobal character of these phosphoryl transfer enzymes, and the deep cleft which is formed between the lobes. A dramatic conformational change occurs in hexokinase as glucose binds to the bottom of the cleft, which causes the two lobes of hexokinase to come together. A substrate-induced closing of the active site cleft is postulated to occur in other kinases as well. This change may provide a mechanism by which some of these enzymes reduce their inherent adenosine triphosphatase activity and could be a general requirement of the kinase reaction.
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Cites
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P1,P5-Di(adenosine-5′)pentaphosphate, a Potent Multisubstrate Inhibitor of Adenylate Kinase
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Self-citationSubstrate positions and induced-fit in crystalline adenylate kinase
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Self-citationThe Amino‐Acid Sequence of Porcine Adenylate Kinase from Skeletal Muscle
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Self-citation
Cited by
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Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
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A database of macromolecular motions
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Metadata
- Authors
- Anderson, C. M., Zucker, F. H., & Steitz, T. A.
- Venue
- Science
- Published
- 1979-04-27
- Volume
- 204
- Issue
- 4391
- Pages
- 375-380
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1996537553
- Cited by
- 277
- References
- 13
- FWCI
- 6.98
- Type
- journal article
- Language
- en
- Open access
- closed
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- Anderson, C. M., Zucker, F. H., & Steitz, T. A. (1979). Space-Filling Models of Kinase Clefts and Conformation Changes: Comparison of the surface structures of kinase enzymes implicates closing clefts in their mechanism. Science. https://doi.org/10.1126/science.220706
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
