Premium
Solution structure of the C4 zinc finger domain of HDM2
Author(s) -
Yu Grace W.,
Allen Mark D.,
Andreeva Antonina,
Fersht Alan R.,
Bycroft Mark
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051927306
Subject(s) - zinc finger , zinc , domain (mathematical analysis) , ring finger domain , lim domain , zinc finger nuclease , computational biology , chemistry , crystallography , biophysics , biology , biochemistry , mathematics , gene , transcription factor , mathematical analysis , organic chemistry
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 β‐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.