Abstract
An N-terminal helical region of the tumor suppressor p53 binds in a hydrophobic cleft of the oncoprotein MDM2. A retroinverso isomer of the natural N-terminal helical peptide was found to interact with MDM2 using the same hydrophobic residues, Phe, Trp, and Leu. We propose that the retroinverso d-peptide adopts a right-handed helical conformation to achieve functional mimicry of the p53 peptide.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Circular Dichroism
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Enzyme-Linked Immunosorbent Assay
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Hydrophobic and Hydrophilic Interactions
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Models, Molecular
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Nuclear Proteins / antagonists & inhibitors*
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Nuclear Proteins / chemistry
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Peptide Fragments / pharmacology*
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Protein Isoforms
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Protein Structure, Secondary
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Proto-Oncogene Proteins / antagonists & inhibitors*
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Proto-Oncogene Proteins / chemistry
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Proto-Oncogene Proteins c-mdm2
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Tumor Suppressor Protein p53 / antagonists & inhibitors
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Tumor Suppressor Protein p53 / chemistry
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Tumor Suppressor Protein p53 / pharmacology*
Substances
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Nuclear Proteins
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Peptide Fragments
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Protein Isoforms
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Proto-Oncogene Proteins
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Tumor Suppressor Protein p53
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Proto-Oncogene Proteins c-mdm2