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Solution structure of the C4 zinc finger domain of HDM2.

ABSTRACT: 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.

SUBMITTER: Yu GW

PROVIDER: S-EPMC2242465 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature

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Solution structure of the C4 zinc finger domain of HDM2.

Yu Grace W GW Allen Mark D MD Andreeva Antonina A Fersht Alan R AR Bycroft Mark M

Protein science : a publication of the Protein Society 20051229 2

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 ...[more]

PMID: 16385008

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