Document Detail

Effects on polo-like kinase 1 polo-box domain binding affinities of peptides incurred by structural variation at the phosphoamino acid position.
MedLine Citation:
PMID:  22743087     Owner:  NLM     Status:  MEDLINE    
Protein-protein interactions (PPIs) mediated by the polo-box domain (PBD) of polo-like kinase 1 (Plk1) serve important roles in cell proliferation. Critical elements in the high affinity recognition of peptides and proteins by PBD are derived from pThr/pSer-residues in the binding ligands. However, there has been little examination of pThr/pSer mimetics within a PBD context. Our current paper compares the abilities of a variety of amino acid residues and derivatives to serve as pThr/pSer replacements by exploring the role of methyl functionality at the pThr β-position and by replacing the phosphoryl group by phosphonic acid, sulfonic acid and carboxylic acids. This work sheds new light on structure activity relationships for PBD recognition of phosphoamino acid mimetics.
Wenjian Qian; Jung-Eun Park; Fa Liu; Kyung S Lee; Terrence R Burke
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Intramural     Date:  2012-05-26
Journal Detail:
Title:  Bioorganic & medicinal chemistry     Volume:  21     ISSN:  1464-3391     ISO Abbreviation:  Bioorg. Med. Chem.     Publication Date:  2013 Jul 
Date Detail:
Created Date:  2013-06-14     Completed Date:  2014-01-21     Revised Date:  2014-08-10    
Medline Journal Info:
Nlm Unique ID:  9413298     Medline TA:  Bioorg Med Chem     Country:  England    
Other Details:
Languages:  eng     Pagination:  3996-4003     Citation Subset:  IM    
Copyright Information:
Published by Elsevier Ltd.
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MeSH Terms
Cell Cycle Proteins / chemistry*,  metabolism
Drug Design
Models, Molecular*
Molecular Structure
Peptides / chemical synthesis,  chemistry*,  metabolism
Phosphoamino Acids / chemical synthesis,  chemistry*,  metabolism
Protein Binding
Protein Structure, Tertiary
Protein-Serine-Threonine Kinases / chemistry*,  metabolism
Proto-Oncogene Proteins / chemistry*,  metabolism
Structure-Activity Relationship
Grant Support
Reg. No./Substance:
0/Cell Cycle Proteins; 0/Peptides; 0/Phosphoamino Acids; 0/Proto-Oncogene Proteins; EC Kinases; EC kinase 1

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