1ctl
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(New page: 200px<br /><applet load="1ctl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ctl" /> '''STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN...)
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Revision as of 10:37, 20 November 2007
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STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH PROTEIN CRP
Overview
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.
About this Structure
1CTL is a Single protein structure of sequence from Gallus gallus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP., Perez-Alvarado GC, Miles C, Michelsen JW, Louis HA, Winge DR, Beckerle MC, Summers MF, Nat Struct Biol. 1994 Jun;1(6):388-98. PMID:7664053
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