Solution structure of the C4 zinc finger domain of HDM2.
HDM2 is a ubiquitin E3 ligase that is a key negative regulator of the tumor suppressor p53. Here, we report the determination of the solution structure of the C4 zinc finger domain of HDM2 using multidimensional NMR. The HDM2 C4 zinc finger domain has a fold consisting of a 3(10) helix followed by four beta-strands, which shares significant structural similarity to the zinc ribbon protein family. Family based sequence analysis identified two putative binding sites, one of which resembles an RNA binding motif.
Yu
Grace W
GW
Centre for Protein Engineering, Medical Research Council, Hills Road, CB2 2QH, Cambridge, United Kingdom.
Allen
Mark D
MD
Andreeva
Antonina
A
Fersht
Alan R
AR
Bycroft
Mark
M
D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D051736:Proto-Oncogene Proteins c-mdm2 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D016335:Zinc Fingers
D012996:Solutions; D051736:Proto-Oncogene Proteins c-mdm2