1ig7

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(New page: 200px<br /><applet load="1ig7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ig7, resolution 2.20&Aring;" /> '''Msx-1 Homeodomain/DN...)
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[[Image:1ig7.gif|left|200px]]<br /><applet load="1ig7" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ig7.gif|left|200px]]<br /><applet load="1ig7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ig7, resolution 2.20&Aring;" />
caption="1ig7, resolution 2.20&Aring;" />
'''Msx-1 Homeodomain/DNA Complex Structure'''<br />
'''Msx-1 Homeodomain/DNA Complex Structure'''<br />
==Overview==
==Overview==
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The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are, comprised of 60 amino acids that show a high degree of evolutionary, conservation. We have determined the structure of the Msx-1 homeodomain, complexed to DNA at 2.2 A resolution. The structure has an unusually, well-ordered N-terminal arm with a unique trajectory across the minor, groove of the DNA. DNA specificity conferred by bases flanking the core, TAAT sequence is explained by well ordered water-mediated interactions at, Q50. Most interactions seen at the TAAT sequence are typical of the, interactions seen in other homeodomain structures. Comparison of the, Msx-1-HD structure to all other high resolution HD-DNA complex structures, indicate a remarkably well-conserved sphere of hydration between the DNA, and protein in these complexes.
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The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are comprised of 60 amino acids that show a high degree of evolutionary conservation. We have determined the structure of the Msx-1 homeodomain complexed to DNA at 2.2 A resolution. The structure has an unusually well-ordered N-terminal arm with a unique trajectory across the minor groove of the DNA. DNA specificity conferred by bases flanking the core TAAT sequence is explained by well ordered water-mediated interactions at Q50. Most interactions seen at the TAAT sequence are typical of the interactions seen in other homeodomain structures. Comparison of the Msx-1-HD structure to all other high resolution HD-DNA complex structures indicate a remarkably well-conserved sphere of hydration between the DNA and protein in these complexes.
==About this Structure==
==About this Structure==
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1IG7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IG7 OCA].
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1IG7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IG7 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Abate-Shen, C.]]
[[Category: Abate-Shen, C.]]
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[[Category: Geiger, J.H.]]
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[[Category: Geiger, J H.]]
[[Category: Hovde, S.]]
[[Category: Hovde, S.]]
[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:22:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:31 2008''

Revision as of 11:11, 21 February 2008


1ig7, resolution 2.20Å

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Msx-1 Homeodomain/DNA Complex Structure

Overview

The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are comprised of 60 amino acids that show a high degree of evolutionary conservation. We have determined the structure of the Msx-1 homeodomain complexed to DNA at 2.2 A resolution. The structure has an unusually well-ordered N-terminal arm with a unique trajectory across the minor groove of the DNA. DNA specificity conferred by bases flanking the core TAAT sequence is explained by well ordered water-mediated interactions at Q50. Most interactions seen at the TAAT sequence are typical of the interactions seen in other homeodomain structures. Comparison of the Msx-1-HD structure to all other high resolution HD-DNA complex structures indicate a remarkably well-conserved sphere of hydration between the DNA and protein in these complexes.

About this Structure

1IG7 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Msx-1 homeodomain/DNA complex., Hovde S, Abate-Shen C, Geiger JH, Biochemistry. 2001 Oct 9;40(40):12013-21. PMID:11580277

Page seeded by OCA on Thu Feb 21 13:11:31 2008

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