2bnx

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(New page: 200px<br /><applet load="2bnx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bnx, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:2bnx.gif|left|200px]]<br /><applet load="2bnx" size="350" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF THE DIMERIC REGULATORY DOMAIN OF MOUSE DIAPHANEOUS-RELATED FORMIN (DRF), MDIA1'''<br />
'''CRYSTAL STRUCTURE OF THE DIMERIC REGULATORY DOMAIN OF MOUSE DIAPHANEOUS-RELATED FORMIN (DRF), MDIA1'''<br />
==Overview==
==Overview==
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Diaphanous-related formins (DRFs) regulate dynamics of unbranched actin, filaments during cell contraction and cytokinesis. DRFs are autoinhibited, through intramolecular binding of a Diaphanous autoinhibitory domain (DAD), to a conserved N-terminal regulatory element. Autoinhibition is relieved, through binding of the GTPase RhoA to the N-terminal element. We report, the crystal structure of the dimeric regulatory domain of the DRF, mDia1., Dimerization is mediated by an intertwined six-helix bundle, from which, extend two Diaphanous inhibitory domains (DIDs) composed of five armadillo, repeats. NMR and biochemical mapping indicate the RhoA and DAD binding, sites on the DID partially overlap, explaining activation of mDia1 by the, GTPase. RhoA binding also requires an additional structurally independent, segment adjacent to the DID. This regulatory construction, involving a, GTPase binding site spanning a flexibly tethered arm and the inhibitory, module, is observed in many autoinhibited effectors of Ras superfamily, GTPases, suggesting evolutionary pressure for this design.
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Diaphanous-related formins (DRFs) regulate dynamics of unbranched actin filaments during cell contraction and cytokinesis. DRFs are autoinhibited through intramolecular binding of a Diaphanous autoinhibitory domain (DAD) to a conserved N-terminal regulatory element. Autoinhibition is relieved through binding of the GTPase RhoA to the N-terminal element. We report the crystal structure of the dimeric regulatory domain of the DRF, mDia1. Dimerization is mediated by an intertwined six-helix bundle, from which extend two Diaphanous inhibitory domains (DIDs) composed of five armadillo repeats. NMR and biochemical mapping indicate the RhoA and DAD binding sites on the DID partially overlap, explaining activation of mDia1 by the GTPase. RhoA binding also requires an additional structurally independent segment adjacent to the DID. This regulatory construction, involving a GTPase binding site spanning a flexibly tethered arm and the inhibitory module, is observed in many autoinhibited effectors of Ras superfamily GTPases, suggesting evolutionary pressure for this design.
==About this Structure==
==About this Structure==
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2BNX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BNX OCA].
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2BNX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BNX OCA].
==Reference==
==Reference==
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[[Category: Otomo, T.]]
[[Category: Otomo, T.]]
[[Category: Rosen, M.]]
[[Category: Rosen, M.]]
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[[Category: Tomchick, D.R.]]
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[[Category: Tomchick, D R.]]
[[Category: CL]]
[[Category: CL]]
[[Category: actin]]
[[Category: actin]]
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[[Category: structural protein]]
[[Category: structural protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:51:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:48 2008''

Revision as of 14:39, 21 February 2008

Image:2bnx.gif

2bnx, resolution 2.40Å

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CRYSTAL STRUCTURE OF THE DIMERIC REGULATORY DOMAIN OF MOUSE DIAPHANEOUS-RELATED FORMIN (DRF), MDIA1

Overview

Diaphanous-related formins (DRFs) regulate dynamics of unbranched actin filaments during cell contraction and cytokinesis. DRFs are autoinhibited through intramolecular binding of a Diaphanous autoinhibitory domain (DAD) to a conserved N-terminal regulatory element. Autoinhibition is relieved through binding of the GTPase RhoA to the N-terminal element. We report the crystal structure of the dimeric regulatory domain of the DRF, mDia1. Dimerization is mediated by an intertwined six-helix bundle, from which extend two Diaphanous inhibitory domains (DIDs) composed of five armadillo repeats. NMR and biochemical mapping indicate the RhoA and DAD binding sites on the DID partially overlap, explaining activation of mDia1 by the GTPase. RhoA binding also requires an additional structurally independent segment adjacent to the DID. This regulatory construction, involving a GTPase binding site spanning a flexibly tethered arm and the inhibitory module, is observed in many autoinhibited effectors of Ras superfamily GTPases, suggesting evolutionary pressure for this design.

About this Structure

2BNX is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis of Rho GTPase-mediated activation of the formin mDia1., Otomo T, Otomo C, Tomchick DR, Machius M, Rosen MK, Mol Cell. 2005 Apr 29;18(3):273-81. PMID:15866170

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