4bkg
crystal structure of human diSUMO-2
Structural highlights
FunctionSUMO2_HUMAN Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.[1] [2] [3] Publication Abstract from PubMedRNF4 [RING (really interesting new gene) finger protein 4] is a SUMO-targeted ubiquitin ligase (STUbL) controlling promyelocytic leukemia (PML) nuclear bodies, DNA double strand break repair and other nuclear functions. We describe that the sequence and spacing of the SUMO-interaction motifs (SIMs) in RNF4 regulate the avidity-driven recognition of substrate proteins carrying SUMO chains of variable length. Multivalent interactions of the SUMO-interaction motifs in the RING-finger protein 4 (RNF4) determine the specificity for chains of the small ubiquitin-related modifier (SUMO).,Keusekotten K, Bade VN, Meyer-Teschendorf K, Sriramachandran AM, Fischer-Schrader K, Krause A, Horst C, Schwarz G, Hofmann K, Dohmen RJ, Praefcke GJ Biochem J. 2013 Oct 23. PMID:24151981[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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