1r2b

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Revision as of 19:52, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1r2b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2b, resolution 2.2Å" /> '''Crystal structure of...)
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File:1r2b.gif


1r2b, resolution 2.2Å

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Crystal structure of the BCL6 BTB domain complexed with a SMRT co-repressor peptide

OverviewOverview

BCL6 encodes a transcription factor that represses genes necessary for the, terminal differentiation of lymphocytes within germinal centers, and the, misregulated expression of this factor is strongly implicated in several, types of B cell lymphoma. The homodimeric BTB domain of BCL6 (also known, as the POZ domain) is required for the repression activity of the protein, and interacts directly with the SMRT and N-CoR corepressors that are found, within large multiprotein histone deacetylase-containing complexes. We, have identified a 17 residue fragment from SMRT that binds to the BCL6 BTB, domain, and determined the crystal structure of the complex to 2.2 A. Two, SMRT fragments bind symmetrically to the BCL6 BTB homodimer and, in, combination with biochemical and in vivo data, the structure provides, insight into the basis of transcriptional repression by this critical B, cell lymphoma protein.

DiseaseDisease

Known diseases associated with this structure: Diabetes mellitus, neonatal, with congenital hypothyroidism OMIM:[610192], Lymphoma, B-cell OMIM:[109565]

About this StructureAbout this Structure

1R2B is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain., Ahmad KF, Melnick A, Lax S, Bouchard D, Liu J, Kiang CL, Mayer S, Takahashi S, Licht JD, Prive GG, Mol Cell. 2003 Dec;12(6):1551-64. PMID:14690607

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