1au7: Difference between revisions
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[[Image:1au7.gif|left|200px]] | [[Image:1au7.gif|left|200px]] | ||
'''PIT-1 MUTANT/DNA COMPLEX''' | {{Structure | ||
|PDB= 1au7 |SIZE=350|CAPTION= <scene name='initialview01'>1au7</scene>, resolution 2.300Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= PIT-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |||
}} | |||
'''PIT-1 MUTANT/DNA COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AU7 is a [ | 1AU7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AU7 OCA]. | ||
==Reference== | ==Reference== | ||
Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility., Jacobson EM, Li P, Leon-del-Rio A, Rosenfeld MG, Aggarwal AK, Genes Dev. 1997 Jan 15;11(2):198-212. PMID:[http:// | Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility., Jacobson EM, Li P, Leon-del-Rio A, Rosenfeld MG, Aggarwal AK, Genes Dev. 1997 Jan 15;11(2):198-212. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9009203 9009203] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:19 2008'' | ||
Revision as of 11:02, 20 March 2008
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| , resolution 2.300Å | |||||||
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| Gene: | PIT-1 (Rattus norvegicus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PIT-1 MUTANT/DNA COMPLEX
OverviewOverview
Pit-1, a member of the POU domain family of transcription factors, characterized by a bipartite DNA-binding domain, serves critical developmental functions based on binding to diverse DNA elements in its target genes. Here we report a high resolution X-ray analysis of the Pit-1 POU domain bound to a DNA element as a homodimer. This analysis reveals that Pit-1 subdomains bind to perpendicular faces of the DNA, rather than opposite faces of the DNA as in Oct-1. This is accomplished by different spacing and orientation of the POU-specific domain. Contrary to previous predictions, the dimerization interface involves the carboxyl terminus of the DNA recognition helix of the homeodomain, which in an extended conformation interacts with specific residues at the amino terminus of helix alpha1 and in the loop between helices alpha3 and alpha4 of the POU-specific domain of the symmetry related monomer. These features suggest the molecular basis of disease-causing mutations in Pit-1 and provide potential basis for the flexible allostery between protein domains and DNA sites in the activation of target genes.
About this StructureAbout this Structure
1AU7 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility., Jacobson EM, Li P, Leon-del-Rio A, Rosenfeld MG, Aggarwal AK, Genes Dev. 1997 Jan 15;11(2):198-212. PMID:9009203
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