Leu628 of the KIX domain of CBP is a key residue for the interaction with the MLL transactivation domain-Reference-Cited by-同舟云学术

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Leu628 of the KIX domain of CBP is a key residue for the interaction with the MLL transactivation domain

Published:2010-10-20 Issue:22 Volume:584 Page:4500-4504
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Arai Munehito,Dyson H. Jane,Wright Peter E.

Funder

National Institutes of Health and the Skaggs Institute for Chemical Biology

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference21 articles.

1. Biological control through regulated transcriptional coactivators;Spiegelman;Cell,2004

2. CBP/p300 in cell growth, transformation, and development;Goodman;Genes Dev.,2000

3. Intrinsically unstructured proteins and their functions;Dyson;Nat. Rev. Mol. Cell Biol.,2005

4. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions;Radhakrishnan;Cell,1997

5. Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain;Goto;J. Biol. Chem.,2002

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1. Garcinolic Acid Distinguishes Between GACKIX Domains and Modulates Interaction Networks;ChemBioChem;2023-09-07

2. Rational peptide design for inhibition of the KIX–MLL interaction;Scientific Reports;2023-04-18

3. Structural and interaction analysis of human lipocalin‐type prostaglandin D synthase with the poorly water‐soluble drug NBQX;The FEBS Journal;2023-04-11

4. Peptide Tethering: Pocket-Directed Fragment Screening for Peptidomimetic Inhibitor Discovery;Journal of the American Chemical Society;2022-01-14

5. A Dual-Site Inhibitor of CBP/p300 KIX is a Selective and Effective Modulator of Myb;Journal of the American Chemical Society;2021-09-07

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