5C0M

Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide

Summary for 5C0M

• Entry DOI: 10.2210/pdb5c0m/pdb
• Descriptor: SAGA-associated factor 29 homolog, Carba-containing peptide, SULFATE ION, ... (6 entities in total)
• Functional Keywords: sgf29, tandem tudor domain, carba containing peptide, structural genomics, structural genomics consortium, sgc, transcription
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q96ES7
• Total number of polymer chains: 4
• Total formula weight: 43068.95

Authors

Dong, A.,Xu, C.,Tempel, W.,Cerovina, T.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2015-06-12, release date: 2015-07-01, Last modification date: 2023-11-15)

Primary citation

Kamps, J.J.,Huang, J.,Poater, J.,Xu, C.,Pieters, B.J.,Dong, A.,Min, J.,Sherman, W.,Beuming, T.,Matthias Bickelhaupt, F.,Li, H.,Mecinovic, J.
Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.
Nat Commun, 6:8911-8911, 2015

PubMed Abstract: A large number of structurally diverse epigenetic reader proteins specifically recognize methylated lysine residues on histone proteins. Here we describe comparative thermodynamic, structural and computational studies on recognition of the positively charged natural trimethyllysine and its neutral analogues by reader proteins. This work provides experimental and theoretical evidence that reader proteins predominantly recognize trimethyllysine via a combination of favourable cation-π interactions and the release of the high-energy water molecules that occupy the aromatic cage of reader proteins on the association with the trimethyllysine side chain. These results have implications in rational drug design by specifically targeting the aromatic cage of readers of trimethyllysine.

PubMed: 26578293
DOI: 10.1038/ncomms9911

Experimental method

X-RAY DIFFRACTION (1.6 Å)