2r5z: Difference between revisions
New page: left|200px<br /><applet load="2r5z" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r5z" /> ''''''<br /> ==About this Structure== is a [h... |
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[[Image:2r5z.jpg|left|200px]]<br /><applet load="2r5z" size="350" color="white" frame="true" align="right" spinBox="true" | [[Image:2r5z.jpg|left|200px]]<br /><applet load="2r5z" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2r5z" /> | caption="2r5z, resolution 2.60Å" /> | ||
''''''<br /> | '''Structure of Scr/Exd complex bound to a DNA sequence derived from the fkh gene'''<br /> | ||
==Overview== | |||
The recognition of specific DNA-binding sites by transcription factors is, a critical yet poorly understood step in the control of gene expression., Members of the Hox family of transcription factors bind DNA by making, nearly identical major groove contacts via the recognition helices of, their homeodomains. In vivo specificity, however, often depends on, extended and unstructured regions that link Hox homeodomains to a, DNA-bound cofactor, Extradenticle (Exd). Using a combination of structure, determination, computational analysis, and in vitro and in vivo assays, we, show that Hox proteins recognize specific Hox-Exd binding sites via, residues located in these extended regions that insert into the minor, groove but only when presented with the correct DNA sequence. Our results, suggest that these residues, which are conserved in a paralog-specific, manner, confer specificity by recognizing a sequence-dependent DNA, structure instead of directly reading a specific DNA sequence. | |||
==About this Structure== | ==About this Structure== | ||
2R5Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5Z OCA]. | |||
==Reference== | |||
Functional specificity of a Hox protein mediated by the recognition of minor groove structure., Joshi R, Passner JM, Rohs R, Jain R, Sosinsky A, Crickmore MA, Jacob V, Aggarwal AK, Honig B, Mann RS, Cell. 2007 Nov 2;131(3):530-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17981120 17981120] | |||
[[Category: Drosophila melanogaster]] | |||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Aggarwal, A.K.]] | |||
[[Category: Jain, R.]] | |||
[[Category: Passner, J.M.]] | |||
[[Category: developmental protein]] | |||
[[Category: dna-binding]] | |||
[[Category: homeobox]] | |||
[[Category: homeodomain]] | |||
[[Category: homeotic proteins]] | |||
[[Category: nucleus]] | |||
[[Category: specificity]] | |||
[[Category: transcription]] | |||
[[Category: transcription regulation]] | |||
[[Category: transcription/dna complex]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 17:23:57 2008'' | ||
Revision as of 18:23, 6 February 2008
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Structure of Scr/Exd complex bound to a DNA sequence derived from the fkh gene
OverviewOverview
The recognition of specific DNA-binding sites by transcription factors is, a critical yet poorly understood step in the control of gene expression., Members of the Hox family of transcription factors bind DNA by making, nearly identical major groove contacts via the recognition helices of, their homeodomains. In vivo specificity, however, often depends on, extended and unstructured regions that link Hox homeodomains to a, DNA-bound cofactor, Extradenticle (Exd). Using a combination of structure, determination, computational analysis, and in vitro and in vivo assays, we, show that Hox proteins recognize specific Hox-Exd binding sites via, residues located in these extended regions that insert into the minor, groove but only when presented with the correct DNA sequence. Our results, suggest that these residues, which are conserved in a paralog-specific, manner, confer specificity by recognizing a sequence-dependent DNA, structure instead of directly reading a specific DNA sequence.
About this StructureAbout this Structure
2R5Z is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
Functional specificity of a Hox protein mediated by the recognition of minor groove structure., Joshi R, Passner JM, Rohs R, Jain R, Sosinsky A, Crickmore MA, Jacob V, Aggarwal AK, Honig B, Mann RS, Cell. 2007 Nov 2;131(3):530-43. PMID:17981120
Page seeded by OCA on Wed Feb 6 17:23:57 2008