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| {{STRUCTURE_2aql| PDB=2aql | SCENE= }} | | {{STRUCTURE_2aql| PDB=2aql | SCENE= }} |
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| '''Crystal Structure of the MRG15 MRG domain'''
| | ===Crystal Structure of the MRG15 MRG domain=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_16407074}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16407074 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16407074}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mrg domain]] | | [[Category: Mrg domain]] |
| [[Category: Recombinase]] | | [[Category: Recombinase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:21:04 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:12:55 2008'' |
