2aql
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(New page: 200px<br /> <applet load="2aql" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aql, resolution 2.30Å" /> '''Crystal Structure o...)
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Revision as of 18:47, 12 November 2007
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Crystal Structure of the MRG15 MRG domain
Overview
The ubiquitous MRG/MORF family of proteins is involved in cell senescence, or the terminal loss of proliferative potential, a model for aging and, tumor suppression at the cellular level. These proteins are defined by the, approximately 20 kDa MRG domain that binds a plethora of transcriptional, regulators and chromatin-remodeling factors, including the histone, deacetylase transcriptional corepressor mSin3A and the novel nuclear, protein PAM14, and they are also known components of the Tip60/NuA4, complex via interactions with the MRG binding protein (MRGBP). We present, here the crystal structure of a prototypic MRG domain from human MRG15, whose core consists of two orthogonal helix hairpins. Despite the lack of, sequence similarity, the core structure has surprisingly striking homology, to a DNA-interacting domain of the tyrosine site-specific recombinases, XerD, lambda integrase, and Cre. Site-directed mutagenesis studies based, on the X-ray structure and bioinformatics identified key residues involved, in the binding of PAM14 and MRGBP.
About this Structure
2AQL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Multipurpose MRG domain involved in cell senescence and proliferation exhibits structural homology to a DNA-interacting domain., Bowman BR, Moure CM, Kirtane BM, Welschhans RL, Tominaga K, Pereira-Smith OM, Quiocho FA, Structure. 2006 Jan;14(1):151-8. PMID:16407074
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