1bc8: Difference between revisions

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[[Image:1bc8.gif|left|200px]]<br />

[[Image:1bc8.gif|left|200px]]<br /><applet load="1bc8" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1bc8" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1bc8, resolution 1.93Å" />

'''STRUCTURES OF SAP-1 BOUND TO DNA SEQUENCES FROM THE E74 AND C-FOS PROMOTERS PROVIDE INSIGHTS INTO HOW ETS PROTEINS DISCRIMINATE BETWEEN RELATED DNA TARGETS'''<br />

==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.

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==

1BC8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1BC8 OCA].

1BC8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC8 OCA].

==Reference==

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[[Category: winged helix-turn-helix]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 16~~:08:~~26 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:43 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1bc8.gif|left|200px]]<br />
+[[Image:1bc8.gif|left|200px]]<br /><applet load="1bc8" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1bc8" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1bc8, resolution 1.93&Aring;" />
 '''STRUCTURES OF SAP-1 BOUND TO DNA SEQUENCES FROM THE E74 AND C-FOS PROMOTERS PROVIDE INSIGHTS INTO HOW ETS PROTEINS DISCRIMINATE BETWEEN RELATED DNA TARGETS'''<br />
 ==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.
+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==
-BC8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BC8 OCA].
+BC8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC8 OCA].
 ==Reference==
@@ Line 25: / Line 24: @@
 [[Category: winged helix-turn-helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:08:26 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:43 2008''