Noncovalent structure of SENP1 in complex with SUMO2

• Published in: Acta crystallographica. Section F, Structural biology communications Vol. 75; no. 5; pp. 332 - 339
• Main Author: Ambaye, Nigus D.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.05.2019; Wiley Subscription Services, Inc
• Subjects: Amino Acid Sequence; Binding Sites; Biological activity; cancer; Catalysis; Cloning, Molecular; Complex formation; Crystallography, X-Ray; Cysteine Endopeptidases - chemistry; Cysteine Endopeptidases - genetics; Cysteine Endopeptidases - metabolism; Escherichia coli - genetics; Escherichia coli - metabolism; Gene Expression; Genetic Vectors - chemistry; Genetic Vectors - metabolism; Humans; Hydrophobicity; Models, Molecular; protease; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Research Communications; SENP; SENP1; Small Ubiquitin-Related Modifier Proteins - chemistry; Small Ubiquitin-Related Modifier Proteins - genetics; Small Ubiquitin-Related Modifier Proteins - metabolism; Structural Homology, Protein; Substrates; SUMO protein; SUMO2; SUMOylation; Thermodynamics; Ubiquitin; X‐ray diffraction; protease; SENP; SUMO2; X-ray diffraction; cancer; SUMOylation; SENP1

SUMOylation is a post‐translational modification in which a small ubiquitin‐like molecule (SUMO) is appended to substrate proteins and is known to influence myriads of biological processes. A delicate interplay between several families of SUMOylation proteins and their substrates ensures the proper...