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PDBsum entry 1ctl
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Metal binding protein
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PDB id
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1ctl
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References listed in PDB file
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Key reference
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Title
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Structure of the carboxy-Terminal lim domain from the cysteine rich protein crp.
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Authors
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G.C.Pérez-Alvarado,
C.Miles,
J.W.Michelsen,
H.A.Louis,
D.R.Winge,
M.C.Beckerle,
M.F.Summers.
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Ref.
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Nat Struct Biol, 1994,
1,
388-398.
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PubMed id
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Abstract
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The three dimensional solution structure of the carboxy terminal LIM domain of
the avian Cysteine Rich Protein (CRP) has been determined by nuclear magnetic
resonance spectroscopy. The domain contains two zinc atoms bound independently
in CCHC (C = Cys, H = His) and CCCC modules. Both modules contain two
orthogonally-arranged antiparallel beta-sheets, and the CCCC module contains an
alpha-helix at its C terminus. The modules pack due to hydrophobic interactions
forming a novel global fold. The structure of the C-terminal CCCC module is
essentially identical to that observed for the DNA-interactive CCCC modules of
the GATA-1 and steroid hormone receptor DNA binding domains, raising the
possibility that the LIM motif may have a DNA binding function.
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