Crystal structure of a PUT3–DNA complex reveals a novel mechanism for DMA recognition by a protein containing a Zn2Cys6 binuclear cluster

By K. Swaminathan, P. Flynn, R. J. Reece, R. Marmorstein. 1997

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

1. Zeynep Kurkcuoglu
2. Alexandre M. J. J. Bonvin
3. R. J. Reece
4. M. V. van Dijk
5. Nelly Andrusier
6. Matthew Menke

Citations in the corpus

• Pushing the limits of what is achievable in protein–DNA docking: benchmarking HADDOCK’s performance (2010, neutral): “Pas: V51,G57,P58,T66,V71,H77, H100,K119 1zme (66) Act: (R9,R11,H12,R80,R82,H83) Pas: A4,K14,K39-S43, A75,K85,K100-S114 Act: (C2,G3,G4,C15,C17,G18, C20,G21,G22,C33,C34,G35) (T26-C32,C9-T14) (67–72)”
• Analysis of Genes and Genomes (2004, methodology): “(c)–(e) The structure, as determined by X-ray crystallography, of the Gal4p-DNA, Put3pDNA and Ppr1p-DNA complexes (Marmorstein et al., 1992; Marmorstein and Harrison, 1994; Swaminathan et al., 1997).”
• Pre‐ and post‐docking sampling of conformational changes using ClustENM and HADDOCK for protein‐protein and protein‐DNA systems (2019, background): “Because of the high charge of DNA, the value for the dielectric constant was set to 78.”