4BKG

crystal structure of human diSUMO-2

Summary for 4BKG

• Entry DOI: 10.2210/pdb4bkg/pdb
• Descriptor: SMALL UBIQUITIN-RELATED MODIFIER 2 (2 entities in total)
• Functional Keywords: protein binding
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 19185.38

Authors

Keusekotten, K.,Bade, V.N.,Meyer-Teschendorf, K.,Sriramachandran, A.,Fischer-Schrader, K.,Krause, A.,Horst, C.,Hofmann, K.,Dohmen, R.J.,Praefcke, G.J.K. (deposition date: 2013-04-25, release date: 2013-11-06, Last modification date: 2023-12-20)

Primary citation

Keusekotten, K.,Bade, V.N.,Meyer-Teschendorf, K.,Sriramachandran, A.M.,Fischer-Schrader, K.,Krause, A.,Horst, C.,Schwarz, G.,Hofmann, K.,Dohmen, R.J.,Praefcke, G.J.
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).
Biochem.J., 457:207-, 2014

PubMed Abstract: RNF4 (RING finger protein 4) is a STUbL [SUMO (small ubiquitin-related modifier)-targeted ubiquitin ligase] controlling PML (promyelocytic leukaemia) nuclear bodies, DNA double strand break repair and other nuclear functions. In the present paper, we describe that the sequence and spacing of the SIMs (SUMO-interaction motifs) in RNF4 regulate the avidity-driven recognition of substrate proteins carrying SUMO chains of variable length.

PubMed: 24151981
DOI: 10.1042/BJ20130753

Experimental method

X-RAY DIFFRACTION (2.11 Å)