2A0T

NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1

Summary for 2A0T

• Entry DOI: 10.2210/pdb2a0t/pdb
• Descriptor: Serine/threonine-protein kinase RAD53, Hypothetical 73.8 kDa protein in SAS3-SEC17 intergenic region, residues 301-310 (2 entities in total)
• Functional Keywords: fha domain. rad53, mdt1, phosphothreonine, phosphoprotein, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P22216; Cytoplasm: P34217
• Total number of polymer chains: 2
• Total formula weight: 18339.66

Authors

Mahajan, A.,Yuan, C.,Pike, B.L.,Heierhorst, J.,Chang, C.-F.,Tsai, M.-D. (deposition date: 2005-06-16, release date: 2005-11-08, Last modification date: 2024-11-13)

Primary citation

Mahajan, A.,Yuan, C.,Pike, B.L.,Heierhorst, J.,Chang, C.-F.,Tsai, M.-D.
FHA Domain-Ligand Interactions: Importance of Integrating Chemical and Biological Approaches
J.Am.Chem.Soc., 127:14572-14573, 2005

PubMed Abstract: Combinatorial library screens based on binding affinity may preferentially select ligands with ability for ionic interactions and miss the biologically relevant ligands that bind more weakly with predominantly hydrophobic interactions.

PubMed: 16231900
DOI: 10.1021/ja054538m

Experimental method

SOLUTION NMR