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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'''STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH PROTEIN CRP'''<br />
'''STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH PROTEIN CRP'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1CTL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CTL OCA].
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1CTL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTL OCA].
==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beckerle, M.C.]]
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[[Category: Beckerle, M C.]]
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[[Category: Louis, H.A.]]
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[[Category: Louis, H A.]]
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[[Category: Michelsen, J.W.]]
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[[Category: Michelsen, J W.]]
[[Category: Miles, C.]]
[[Category: Miles, C.]]
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[[Category: Perez-Alvarado, G.C.]]
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[[Category: Perez-Alvarado, G C.]]
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[[Category: Summers, M.F.]]
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[[Category: Summers, M F.]]
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[[Category: Winge, D.R.]]
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[[Category: Winge, D R.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: lim domain containing proteins]]
[[Category: lim domain containing proteins]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:44:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:33 2008''

Revision as of 10:09, 21 February 2008


1ctl

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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 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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