Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 11
pubmed:dateCreated
2006-3-2
pubmed:abstractText
Pax6 is a member of the Pax family of transcription factors and is essential for eye development. Pax6 has two DNA-binding domains: the paired domain and the homeodomain. The Pax6 paired domain is involved in Pax6 gene autoregulation by binding to its enhancer. In this study, crystallization and preliminary X-ray diffraction analysis of the mammalian Pax6 paired domain in complex with the Pax6 gene enhancer was attempted. The Pax6 paired domain complexed with an optimized 25 bp DNA fragment was crystallized by the hanging-drop vapour-diffusion method. The crystal diffracted synchrotron radiation to 3.0/3.7 A resolution and belongs to the monoclinic space group P2(1), with unit-cell parameters a = 62.21, b = 70.69, c = 176.03 A, beta = 90.54 degrees. Diffraction data were collected to 3.7 A resolution.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-10051657, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-10346815, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-11222774, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-11358870, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-11502253, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-12141441, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-12386935, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-12710953, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-1302030, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-15289432, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-1684639, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-7671301, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-7753863, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-7753864, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-7823934, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-7892602, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-7914031, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-8132558, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-8692913, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-8787739, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-9159393, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-9297966, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511221-9710641
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1009-12
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:16511221-Binding Sites, pubmed-meshheading:16511221-Cloning, Molecular, pubmed-meshheading:16511221-Crystallization, pubmed-meshheading:16511221-Crystallography, X-Ray, pubmed-meshheading:16511221-DNA, pubmed-meshheading:16511221-DNA, Complementary, pubmed-meshheading:16511221-Databases, Protein, pubmed-meshheading:16511221-Diffusion, pubmed-meshheading:16511221-Enhancer Elements, Genetic, pubmed-meshheading:16511221-Escherichia coli, pubmed-meshheading:16511221-Eye Proteins, pubmed-meshheading:16511221-Gene Expression Regulation, pubmed-meshheading:16511221-Homeodomain Proteins, pubmed-meshheading:16511221-Humans, pubmed-meshheading:16511221-Molecular Conformation, pubmed-meshheading:16511221-Oligonucleotides, pubmed-meshheading:16511221-Paired Box Transcription Factors, pubmed-meshheading:16511221-Protein Binding, pubmed-meshheading:16511221-Protein Structure, Tertiary, pubmed-meshheading:16511221-Recombinant Fusion Proteins, pubmed-meshheading:16511221-Repressor Proteins, pubmed-meshheading:16511221-Synchrotrons, pubmed-meshheading:16511221-X-Ray Diffraction
pubmed:year
2005
pubmed:articleTitle
Crystallization and preliminary X-ray analysis of the Pax6 paired domain bound to the Pax6 gene enhancer.
pubmed:affiliation
Department of Structural Biology, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan. morikawa@beri.or.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't