1c7u

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(New page: 200px<br /> <applet load="1c7u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c7u" /> '''Complex of the DNA binding core domain of t...)
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'''Complex of the DNA binding core domain of the transcription factor MEF2A with a 20mer oligonucleotide'''<br />
'''Complex of the DNA binding core domain of the transcription factor MEF2A with a 20mer oligonucleotide'''<br />
==Overview==
==Overview==
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The solution structure of the 33 kDa complex between the dimeric, DNA-binding core domain of the transcription factor MEF2A (residues 1-85), and a 20mer DNA oligonucleotide comprising the consensus sequence, CTA(A/T)(4)TAG has been solved by NMR. The protein comprises two domains:, a MADS-box (residues 1-58) and a MEF2S domain (residues 59-73)., Recognition and specificity are achieved by interactions between the, MADS-box and both the major and minor grooves of the DNA. A number of, critical differences in protein-DNA contacts observed in the MEF2A-DNA, complex and the DNA complexes of the related MADS-box transcription, factors SRF and MCM1 provide a molecular explanation for modulation of, sequence specificity and extent of DNA bending ( approximately 15 versus, approximately 70 degrees ). The structure of the MEF2S domain is entirely, different from that of the equivalent SAM domain in SRF and MCM1, accounting for the absence of cross-reactivity with other proteins that, interact with these transcription factors.
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The solution structure of the 33 kDa complex between the dimeric DNA-binding core domain of the transcription factor MEF2A (residues 1-85) and a 20mer DNA oligonucleotide comprising the consensus sequence CTA(A/T)(4)TAG has been solved by NMR. The protein comprises two domains: a MADS-box (residues 1-58) and a MEF2S domain (residues 59-73). Recognition and specificity are achieved by interactions between the MADS-box and both the major and minor grooves of the DNA. A number of critical differences in protein-DNA contacts observed in the MEF2A-DNA complex and the DNA complexes of the related MADS-box transcription factors SRF and MCM1 provide a molecular explanation for modulation of sequence specificity and extent of DNA bending ( approximately 15 versus approximately 70 degrees ). The structure of the MEF2S domain is entirely different from that of the equivalent SAM domain in SRF and MCM1, accounting for the absence of cross-reactivity with other proteins that interact with these transcription factors.
==About this Structure==
==About this Structure==
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1C7U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C7U OCA].
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1C7U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C7U OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Clore, G.M.]]
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[[Category: Clore, G M.]]
[[Category: Huang, K.]]
[[Category: Huang, K.]]
[[Category: dna binding protein]]
[[Category: dna binding protein]]
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[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:18:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:17 2008''

Revision as of 10:03, 21 February 2008


1c7u

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Complex of the DNA binding core domain of the transcription factor MEF2A with a 20mer oligonucleotide

Overview

The solution structure of the 33 kDa complex between the dimeric DNA-binding core domain of the transcription factor MEF2A (residues 1-85) and a 20mer DNA oligonucleotide comprising the consensus sequence CTA(A/T)(4)TAG has been solved by NMR. The protein comprises two domains: a MADS-box (residues 1-58) and a MEF2S domain (residues 59-73). Recognition and specificity are achieved by interactions between the MADS-box and both the major and minor grooves of the DNA. A number of critical differences in protein-DNA contacts observed in the MEF2A-DNA complex and the DNA complexes of the related MADS-box transcription factors SRF and MCM1 provide a molecular explanation for modulation of sequence specificity and extent of DNA bending ( approximately 15 versus approximately 70 degrees ). The structure of the MEF2S domain is entirely different from that of the equivalent SAM domain in SRF and MCM1, accounting for the absence of cross-reactivity with other proteins that interact with these transcription factors.

About this Structure

1C7U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors., Huang K, Louis JM, Donaldson L, Lim FL, Sharrocks AD, Clore GM, EMBO J. 2000 Jun 1;19(11):2615-28. PMID:10835359

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