The DOI matches its Crossref record; 105 of the 105 references it cites were found in a registry or an index.
Phosphate Recognition in Structural Biology
Abstract
Drug‐discovery research in the past decade has seen an increased selection of targets with phosphate recognition sites, such as protein kinases and phosphatases, in the past decade. This review attempts, with the help of database‐mining tools, to give an overview of the most important principles in molecular recognition of phosphate groups by enzymes. A total of 3003 X‐ray crystal structures from the RCSB Protein Data Bank with bound organophosphates has been analyzed individually, in particular for H‐bonding interactions between proteins and ligands. The various known binding motifs for phosphate binding are reviewed, and similarities to phosphate complexation by synthetic receptors are highlighted. An analysis of the propensities of amino acids in various classes of phosphate‐binding enzymes showed characteristic distributions of amino acids used for phosphate binding. This review demonstrates that structure‐based lead development and optimization should carefully address the phosphate‐binding‐site environment and also proposes new alternatives for filling such sites.
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Recognition and sensing of fluoride anion
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Artificial Receptors for the Recognition of Phosphorylated Molecules
Hargrove, A. E., Nieto, S., Zhang, T., Sessler, J. L., & Anslyn, E. V. (2011) · Chemical Reviews · doi:10.1021/cr100242s · Cited by 649
The Alkaline Solution to the Emergence of Life: Energy, Entropy and Early Evolution
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Metadata
- Authors
- Hirsch, A. K. H., Fischer, F. R., & Diederich, F.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2006-12-27
- Volume
- 46
- Issue
- 3
- Pages
- 338-352
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2126374515
- Cited by
- 287
- References
- 105
- FWCI
- 20.50
- Type
- journal article
- Language
- en
- Open access
- closed
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