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1bc7

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(New page: 200px<br /> <applet load="1bc7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bc7, resolution 2.01&Aring;" /> '''SERUM RESPONSE FACT...)
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'''SERUM RESPONSE FACTOR ACCESSORY PROTEIN 1A (SAP-1)/DNA COMPLEX'''<br />
'''SERUM RESPONSE FACTOR ACCESSORY PROTEIN 1A (SAP-1)/DNA COMPLEX'''<br />
==Overview==
==Overview==
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SAP-1 is a member of the Ets transcription factors and cooperates with SRF, protein to activate transcription of the c-fos protooncogene. The crystal, structures of the conserved ETS domain of SAP-1 bound to DNA sequences, from the E74 and c-fos promoters reveal that a set of conserved residues, contact a GGA core DNA sequence. Discrimination for sequences outside this, core is mediated by DNA contacts from conserved and nonconserved protein, residues and sequence-dependent DNA structural properties characteristic, of A-form DNA structure. Comparison with the related PU.1/DNA and, GABPalpha/beta/DNA complexes provides general insights into DNA, discrimination between Ets proteins. Modeling studies of a SAP-1/SRF/DNA, complex suggest that SRF may modulate SAP-1 binding to DNA by interacting, with its ETS domain.
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SAP-1 is a member of the Ets transcription factors and cooperates with SRF protein to activate transcription of the c-fos protooncogene. The crystal structures of the conserved ETS domain of SAP-1 bound to DNA sequences from the E74 and c-fos promoters reveal that a set of conserved residues contact a GGA core DNA sequence. Discrimination for sequences outside this core is mediated by DNA contacts from conserved and nonconserved protein residues and sequence-dependent DNA structural properties characteristic of A-form DNA structure. Comparison with the related PU.1/DNA and GABPalpha/beta/DNA complexes provides general insights into DNA discrimination between Ets proteins. Modeling studies of a SAP-1/SRF/DNA complex suggest that SRF may modulate SAP-1 binding to DNA by interacting with its ETS domain.
==About this Structure==
==About this Structure==
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1BC7 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=1BC7 OCA].
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1BC7 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=1BC7 OCA].
==Reference==
==Reference==
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[[Category: winged helix-turn-helix]]
[[Category: winged helix-turn-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:08:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:44 2008''

Revision as of 09:53, 21 February 2008


1bc7, resolution 2.01Å

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SERUM RESPONSE FACTOR ACCESSORY PROTEIN 1A (SAP-1)/DNA COMPLEX

Overview

SAP-1 is a member of the Ets transcription factors and cooperates with SRF protein to activate transcription of the c-fos protooncogene. The crystal structures of the conserved ETS domain of SAP-1 bound to DNA sequences from the E74 and c-fos promoters reveal that a set of conserved residues contact a GGA core DNA sequence. Discrimination for sequences outside this core is mediated by DNA contacts from conserved and nonconserved protein residues and sequence-dependent DNA structural properties characteristic of A-form DNA structure. Comparison with the related PU.1/DNA and GABPalpha/beta/DNA complexes provides general insights into DNA discrimination between Ets proteins. Modeling studies of a SAP-1/SRF/DNA complex suggest that SRF may modulate SAP-1 binding to DNA by interacting with its ETS domain.

About this Structure

1BC7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structures of SAP-1 bound to DNA targets from the E74 and c-fos promoters: insights into DNA sequence discrimination by Ets proteins., Mo Y, Vaessen B, Johnston K, Marmorstein R, Mol Cell. 1998 Aug;2(2):201-12. PMID:9734357

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