Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases.
Journal, issue, pages	Nucleic Acids Res., Vol. 40, Page 4237-4246, Year 2012
Publish date	Nov 30, 2011 (structure data deposition date)
Authors	Zhang, P. / Lee, H. / Brunzelle, J.S. / Couture, J.F.
External links	Nucleic Acids Res. / PubMed:22266653
Methods	X-ray diffraction
Resolution	1.4 - 2.2 Å
Structure data	PDB-3uvk: Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL2 Method: X-RAY DIFFRACTION / Resolution: 1.4 Å PDB-3uvl: Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL3 Method: X-RAY DIFFRACTION / Resolution: 2.2 Å PDB-3uvm: Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4 Method: X-RAY DIFFRACTION / Resolution: 1.57 Å PDB-3uvn: Crystal structure of WDR5 in complex with the WDR5-interacting motif of SET1A Method: X-RAY DIFFRACTION / Resolution: 1.792 Å PDB-3uvo: Crystal structure of WDR5 in complex with the WDR5-interacting motif of SET1B Method: X-RAY DIFFRACTION / Resolution: 2.2 Å
Chemicals	ChemComp-BTB: 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH bufferYM ChemComp-SO4: SULFATE ION ChemComp-HOH*: WATER
Source	homo sapiens (human)
Keywords	TRANSCRIPTION / trithorax / chromatin biology / beta-propeller / scaffolding / histone H3 / nucleus