2JUO

GABPa OST domain

Summary for 2JUO

• Entry DOI: 10.2210/pdb2juo/pdb
• NMR Information: BMRB: 15451
• Descriptor: GA-binding protein alpha chain (1 entity in total)
• Functional Keywords: ost, ubiquitin, transcription factor, nmr ensemble, ga-binding protein, dna-binding, nucleus, transcription regulation, transcription
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 9975.39

Authors

Kang, H.,Nelson, M.L.,Mackereth, C.D.,Schaerpf, M.,Graves, B.J.,McIntosh, L.P. (deposition date: 2007-08-31, release date: 2008-04-08, Last modification date: 2024-05-08)

Primary citation

Kang, H.S.,Nelson, M.L.,Mackereth, C.D.,Scharpf, M.,Graves, B.J.,McIntosh, L.P.
Identification and structural characterization of a CBP/p300-binding domain from the ETS family transcription factor GABP alpha
J.Mol.Biol., 377:636-646, 2008

PubMed Abstract: Using NMR spectroscopy, we identified and characterized a previously unrecognized structured domain near the N-terminus (residues 35-121) of the ETS family transcription factor GABP alpha. The monomeric domain folds as a five-stranded beta-sheet crossed by a distorted helix. Although globally resembling ubiquitin, the GABP alpha fragment differs in its secondary structure topology and thus appears to represent a new protein fold that we term the OST (On-SighT) domain. The surface of the GABP alpha OST domain contains two predominant clusters of negatively-charged residues suggestive of electrostatically driven interactions with positively-charged partner proteins. Following a best-candidate approach to identify such a partner, we demonstrated through NMR-monitored titrations and glutathione S-transferase pulldown assays that the OST domain binds to the CH1 and CH3 domains of the co-activator histone acetyltransferase CBP/p300. This provides a direct structural link between GABP and a central component of the transcriptional machinery.

PubMed: 18295234
DOI: 10.1016/j.jmb.2008.01.054

Experimental method

SOLUTION NMR