4BKG

crystal structure of human diSUMO-2

4BKG の概要

• エントリーDOI: 10.2210/pdb4bkg/pdb
• 分子名称: SMALL UBIQUITIN-RELATED MODIFIER 2 (2 entities in total)
• 機能のキーワード: protein binding
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19185.38

構造登録者

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. (登録日: 2013-04-25, 公開日: 2013-11-06, 最終更新日: 2023-12-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.11 Å)