Intrinsically unstructured domains of Arf and Hdm2 form bimolecular oligomeric structures in vitro and in vivo.

Sivakolundu, Sivashankar G; Nourse, Amanda; Moshiach, Simon; Bothner, Brian; Ashley, Chimere; Satumba, John; Lahti, Jill; Kriwacki, Richard W

Sivakolundu, Sivashankar G; Nourse, Amanda; Moshiach, Simon; Bothner, Brian; Ashley, Chimere; Satumba, John; Lahti, Jill; Kriwacki, Richard W.

Affiliation

Sivakolundu SG; Department of Structural Biology, St. Jude Children's Research Hospital, 332 North Lauderdale Street, Memphis, TN 38105, USA.

J Mol Biol ; 384(1): 240-54, 2008 Dec 05.

Article in En | MEDLINE | ID: mdl-18809412

Subject(s)

Proto-Oncogene Proteins c-mdm2/chemistry; Tumor Suppressor Protein p14ARF/chemistry; 3T3 Cells; Amino Acid Sequence; Animals; Cell Nucleolus/metabolism; Conserved Sequence; Fibroblasts/cytology; Fibroblasts/metabolism; Humans; Magnetic Resonance Spectroscopy; Mice; Models, Molecular; Molecular Sequence Data; Protein Folding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Proto-Oncogene Proteins c-mdm2/metabolism; Sequence Alignment; Spin Labels; Tumor Suppressor Protein p14ARF/metabolism

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Full text: 1 Database: MEDLINE Main subject: Tumor Suppressor Protein p14ARF / Proto-Oncogene Proteins c-mdm2 Limits: Animals / Humans Language: En Year: 2008 Type: Article

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