Clefts, grooves, and (small) pockets: the structure of the retinoblastoma tumor suppressor in complex with its cellular target E2F unveiled.
Munger
Karl
K
Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Armenise Research Building 544A, Boston, MA 02115-5701, USA. karl_munger@hms.harvard.edu
D000818:Animals; D001665:Binding Sites; D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D050684:E2F Transcription Factors; D006801:Humans; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D016160:Retinoblastoma Protein / Q000737:chemistry*; D015398:Signal Transduction; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics
D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D050684:E2F Transcription Factors; D016160:Retinoblastoma Protein; D014157:Transcription Factors