6pax: Difference between revisions
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'''CRYSTAL STRUCTURE OF THE HUMAN PAX-6 PAIRED DOMAIN-DNA COMPLEX REVEALS A GENERAL MODEL FOR PAX PROTEIN-DNA INTERACTIONS''' | '''CRYSTAL STRUCTURE OF THE HUMAN PAX-6 PAIRED DOMAIN-DNA COMPLEX REVEALS A GENERAL MODEL FOR PAX PROTEIN-DNA INTERACTIONS''' | ||
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[[Category: Xu, H E.]] | [[Category: Xu, H E.]] | ||
[[Category: Xu, W.]] | [[Category: Xu, W.]] | ||
[[Category: | [[Category: Paired domain]] | ||
[[Category: | [[Category: Pax]] | ||
[[Category: | [[Category: Protein-dna interaction]] | ||
[[Category: | [[Category: Transcription]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:42:11 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 22:42, 4 May 2008
CRYSTAL STRUCTURE OF THE HUMAN PAX-6 PAIRED DOMAIN-DNA COMPLEX REVEALS A GENERAL MODEL FOR PAX PROTEIN-DNA INTERACTIONS
OverviewOverview
Pax6, a transcription factor containing the bipartite paired DNA-binding domain, has critical roles in development of the eye, nose, pancreas, and central nervous system. The 2.5 A structure of the human Pax6 paired domain with its optimal 26-bp site reveals extensive DNA contacts from the amino-terminal subdomain, the linker region, and the carboxy-terminal subdomain. The Pax6 structure not only confirms the docking arrangement of the amino-terminal subdomain as seen in cocrystals of the Drosophila Prd Pax protein, but also reveals some interesting differences in this region and helps explain the sequence specificity of paired domain-DNA recognition. In addition, this structure gives the first detailed information about how the paired linker region and carboxy-terminal subdomain contact DNA. The extended linker makes minor groove contacts over an 8-bp region, and the carboxy-terminal helix-turn-helix unit makes base contacts in the major groove. The structure and docking arrangement of the carboxy-terminal subdomain of Pax6 is remarkably similar to that of the amino-terminal subdomain, and there is an approximate twofold symmetry axis relating the polypeptide backbones of these two helix-turn-helix units. Our structure of the Pax6 paired domain-DNA complex provides a framework for understanding paired domain-DNA interactions, for analyzing mutations that map in the linker and carboxy-terminal regions of the paired domain, and for modeling protein-protein interactions of the Pax family proteins.
DiseaseDisease
Known disease associated with this structure: Aniridia, type II OMIM:[607108], Cataract, congenital, with late-onset corneal dystrophy OMIM:[607108], Coloboma, ocular OMIM:[607108], Ectopia pupillae OMIM:[607108], Eye anomalies, multiplex OMIM:[607108], Foveal hypoplasia, isolated OMIM:[607108], Keratitis OMIM:[607108], Morning glory disc anomaly OMIM:[607108], Optic nerve hypoplasia/aplasia OMIM:[607108], Peters anomaly OMIM:[607108]
About this StructureAbout this Structure
6PAX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the human Pax6 paired domain-DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding., Xu HE, Rould MA, Xu W, Epstein JA, Maas RL, Pabo CO, Genes Dev. 1999 May 15;13(10):1263-75. PMID:10346815 Page seeded by OCA on Sun May 4 22:42:11 2008