Conformational dynamics of the Hop1 HORMA domain reveal a common mechanism with the spindle checkpoint protein Mad2

• Published in: Nucleic acids research Vol. 46; no. 1; pp. 279 - 292
• Main Authors: West, Alan M V, Komives, Elizabeth A, Corbett, Kevin D
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 09.01.2018
• Subjects: Amino Acid Sequence; Binding Sites - genetics; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Genome Integrity, Repair and; M Phase Cell Cycle Checkpoints; Mad2 Proteins - chemistry; Mad2 Proteins - genetics; Mad2 Proteins - metabolism; Models, Molecular; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; Protein Binding; Protein Domains; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Sequence Homology, Amino Acid

Abstract The HORMA domain is a highly conserved protein-protein interaction module found in eukaryotic signaling proteins including the spindle assembly checkpoint protein Mad2 and the meiotic HORMAD proteins. HORMA domain proteins interact with short 'closure motifs' in partner proteins b...