2agh
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(New page: 200px<br /> <applet load="2agh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2agh" /> '''Structural basis for cooperative transcript...)
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Revision as of 18:44, 12 November 2007
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Structural basis for cooperative transcription factor binding to the CBP coactivator
Contents |
Overview
Regulation of transcription requires interactions between transcriptional, activators and transcriptional co-activator CREB binding protein (CBP)., The KIX domain of CBP can bind simultaneously to two different proteins, providing an additional mechanism for transcriptional regulation. Here we, describe the solution structure of the ternary complex formed by, cooperative binding of activation domains from the c-Myb and mixed lineage, leukemia (MLL) transcription factors to the KIX domain. The MLL and c-Myb, domains form helices that bind to two distinct hydrophobic grooves on, opposite faces of KIX. Compared to the binary KIX:c-Myb complex, significant changes are observed in the structure of KIX at the MLL, binding interface in the ternary complex. Two regions of KIX that are, disordered in the binary complex become structured in the ternary complex:, a flexible loop forms intimate contacts with bound MLL, and the C-terminal, helix is extended and stabilized by MLL binding. This structural change, results in the formation of additional electrostatic/polar interactions, between KIX and the bound c-Myb, providing a structural basis for the, cooperativity observed for the ternary complex.
Disease
Known diseases associated with this structure: Leukemia, myeloid/lymphoid or mixed-lineage OMIM:[159555]
About this Structure
2AGH is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for cooperative transcription factor binding to the CBP coactivator., De Guzman RN, Goto NK, Dyson HJ, Wright PE, J Mol Biol. 2006 Feb 3;355(5):1005-13. Epub 2005 Oct 5. PMID:16253272
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