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• W2023618084 endingPage "963" @default.
• W2023618084 startingPage "957" @default.
• W2023618084 abstract "It is shown here that the N-terminal domain of MDM2, which is not thought to bind calcium ions, otherwise bears a striking resemblance to a cluster of four EF-hand modules like those found in the calmodulin family. There are similarities in module arrangement, supersecondary structure and the main-chain to main-chain hydrogen-bonding pattern, especially in the vicinity of the short antiparallel beta-sheet, the two strands of which lie between the two E and F helices of tandem modules. Some conserved amino acid residues are identified that are associated with short side-chain to main-chain hydrogen-bonded motifs. Also, both types of domain bind a short, functionally important hydrophobic alpha-helix from another protein in a cavity between the two pairs of EF-hand, or EF-hand-like, modules." @default.
• W2023618084 created "2016-06-24" @default.
• W2023618084 creator A5039952435 @default.
• W2023618084 date "1999-10-01" @default.
• W2023618084 modified "2023-10-16" @default.
• W2023618084 title "The N-terminal domain of MDM2 resembles calmodulin and its relatives 1 1Edited by J. M. Thornton" @default.
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• W2023618084 doi "https://doi.org/10.1006/jmbi.1999.3125" @default.
• W2023618084 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10512695" @default.
• W2023618084 hasPublicationYear "1999" @default.
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