| Autor: |
Yu GW; Centre for Protein Engineering, Medical Research Council, Hills Road, CB2 2QH, Cambridge, United Kingdom., Allen MD, Andreeva A, Fersht AR, Bycroft M |
| Jazyk: |
angličtina |
| Zdroj: |
Protein science : a publication of the Protein Society [Protein Sci] 2006 Feb; Vol. 15 (2), pp. 384-9. Date of Electronic Publication: 2005 Dec 29. |
| DOI: |
10.1110/ps.051927306 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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