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PDBsum entry 2c6b
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References listed in PDB file
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Key reference
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Title
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Solution structure of the c4 zinc finger domain of hdm2.
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Authors
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G.W.Yu,
M.D.Allen,
A.Andreeva,
A.R.Fersht,
M.Bycroft.
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Ref.
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Protein Sci, 2006,
15,
384-389.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
NMR structures of the cis and trans forms of the HDM2 C4 zinc
finger domain. An overlay of the backbone atoms of the 20 lowest
energy NMR structures for the (A) trans and (B) cis forms of the
HDM2 C4 zinc finger. (C) A ribbon representation of the trans
(blue) and cis (red) conformers superimposed over the folded
region, prepared using the program MOLSCRIPT (Kraulis 1991).
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Figure 3.
Comparison of zinc knuckles of HDM2 and Isoleucyl-tRNA
synthetase. (A) MDM2; (B) Isoleucyl-tRNA synthetase (1ffy:A)
boundto tRNA. Conserved Trp, Arg, and Cys are shown as sticks.
The figure was produced using Pymol (DeLanoScientific).
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The above figures are
reprinted
from an Open Access publication published by the Protein Society:
Protein Sci
(2006,
15,
384-389)
copyright 2006.
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