The p53 cofactor Strap exhibits an unexpected TPR motif and oligonucleotide-binding (OB)-fold structure.

Adams, Cassandra J; Pike, Ashley C W; Maniam, Sandra; Sharpe, Timothy D; Coutts, Amanda S; Knapp, Stefan; La Thangue, Nicholas B; Bullock, Alex N

Adams, Cassandra J; Pike, Ashley C W; Maniam, Sandra; Sharpe, Timothy D; Coutts, Amanda S; Knapp, Stefan; La Thangue, Nicholas B; Bullock, Alex N.

Affiliation

Adams CJ; Laboratory of Cancer Biology, Department of Oncology, Medical Sciences Division, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford, OX3 7DQ, United Kingdom.

Proc Natl Acad Sci U S A ; 109(10): 3778-83, 2012 Mar 06.

Article in En | MEDLINE | ID: mdl-22362889

Subject(s)

Carrier Proteins/chemistry; Chromatin/chemistry; Genes, p53; Neoplasm Proteins/chemistry; Oligonucleotides/chemistry; Tumor Suppressor Protein p53/chemistry; Amino Acid Motifs; Animals; Carrier Proteins/metabolism; Crystallography, X-Ray/methods; DNA Damage; E1A-Associated p300 Protein/metabolism; Humans; Mice; Models, Molecular; Neoplasm Proteins/metabolism; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; RNA-Binding Proteins

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oligonucleotides / Chromatin / Carrier Proteins / Genes, p53 / Tumor Suppressor Protein p53 / Neoplasm Proteins Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: Proc Natl Acad Sci U S A Year: 2012 Document type: Article Affiliation country: United kingdom

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