1l8r

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==Overview==
==Overview==
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The Dachshund proteins are essential components of a regulatory network, controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development. These proteins cannot be assigned to, any recognizable structural or functional class based on amino acid, sequence analysis. The 1.65 A crystal structure of the most conserved, domain of human DACHSHUND is reported here. The protein forms an, alpha/beta structure containing a DNA binding motif similar to that found, in the winged helix/forkhead subgroup of the helix-turn-helix family. This, unexpected finding alters the previously proposed molecular models for the, role of Dachshund in the eye determination pathway. Furthermore, it, provides a rational framework for future mechanistic analyses of the, Dachshund proteins in several developmental contexts.
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The Dachshund proteins are essential components of a regulatory network controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development. These proteins cannot be assigned to any recognizable structural or functional class based on amino acid sequence analysis. The 1.65 A crystal structure of the most conserved domain of human DACHSHUND is reported here. The protein forms an alpha/beta structure containing a DNA binding motif similar to that found in the winged helix/forkhead subgroup of the helix-turn-helix family. This unexpected finding alters the previously proposed molecular models for the role of Dachshund in the eye determination pathway. Furthermore, it provides a rational framework for future mechanistic analyses of the Dachshund proteins in several developmental contexts.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Braunstein, S.E.]]
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[[Category: Braunstein, S E.]]
[[Category: Cvekl, A.]]
[[Category: Cvekl, A.]]
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[[Category: Hegde, R.S.]]
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[[Category: Hegde, R S.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
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[[Category: Kim, S.S.]]
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[[Category: Kim, S S.]]
[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
[[Category: winged-helix]]
[[Category: winged-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:17:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:38 2008''

Revision as of 11:42, 21 February 2008


1l8r, resolution 1.65Å

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Structure of the Retinal Determination Protein Dachshund Reveals a DNA-Binding Motif

Overview

The Dachshund proteins are essential components of a regulatory network controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development. These proteins cannot be assigned to any recognizable structural or functional class based on amino acid sequence analysis. The 1.65 A crystal structure of the most conserved domain of human DACHSHUND is reported here. The protein forms an alpha/beta structure containing a DNA binding motif similar to that found in the winged helix/forkhead subgroup of the helix-turn-helix family. This unexpected finding alters the previously proposed molecular models for the role of Dachshund in the eye determination pathway. Furthermore, it provides a rational framework for future mechanistic analyses of the Dachshund proteins in several developmental contexts.

About this Structure

1L8R is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the retinal determination protein Dachshund reveals a DNA binding motif., Kim SS, Zhang RG, Braunstein SE, Joachimiak A, Cvekl A, Hegde RS, Structure. 2002 Jun;10(6):787-95. PMID:12057194

Page seeded by OCA on Thu Feb 21 13:42:38 2008

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