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Published online before print December 29, 2005, 10.1110/ps.051927306
Protein Science (2006), 15:384-389. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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PROTEIN STRUCTURE REPORT

Solution structure of the C4 zinc finger domain of HDM2

Grace W. Yu, Mark D. Allen, Antonina Andreeva, Alan R. Fersht and Mark Bycroft

Centre for Protein Engineering, Medical Research Council, CB2 2QH, Cambridge, United Kingdom

(RECEIVED October 24, 2005; FINAL REVISION October 24, 2005; ACCEPTED November 2, 2005)

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 310 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.

Keywords: HDM2; p53; zinc finger; NMR

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051927306.

Reprint requests to: Mark Bycroft, Centre for Protein Engineering, Medical Research Council, Hills Road, CB2 2QH, Cambridge, United Kingdom; e-mail: mb10031{at}cus.cam.ac.uk; fax: +44-1223-402-140.


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