4ABM

Crystal Structure of CHMP4B hairpin

4ABM の概要

• エントリーDOI: 10.2210/pdb4abm/pdb
• 分子名称: CHARGED MULTIVESICULAR BODY PROTEIN 4B (2 entities in total)
• 機能のキーワード: cell cycle, protein transport, hiv-1
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm, cytosol : Q9H444
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 36998.58

構造登録者

Martinelli, N.,Hartlieb, B.,Usami, Y.,Sabin, C.,Dordor, A.,Ribeiro, E.A.,Gottlinger, H.,Weissenhorn, W. (登録日: 2011-12-08, 公開日: 2012-05-09, 最終更新日: 2024-05-08)

主引用文献

Martinelli, N.,Hartlieb, B.,Usami, Y.,Sabin, C.,Dordor, A.,Miguet, N.,Avilov, S.V.,Ribeiro, E.A.,Gottlinger, H.,Weissenhorn, W.
Cc2D1A is a Regulator of Escrt-III Chmp4B.
J.Mol.Biol., 419:75-, 2012

PubMed Abstract: Endosomal sorting complexes required for transport (ESCRTs) regulate diverse processes ranging from receptor sorting at endosomes to distinct steps in cell division and budding of some enveloped viruses. Common to all processes is the membrane recruitment of ESCRT-III that leads to membrane fission. Here, we show that CC2D1A is a novel regulator of ESCRT-III CHMP4B function. We demonstrate that CHMP4B interacts directly with CC2D1A and CC2D1B with nanomolar affinity by forming a 1:1 complex. Deletion mapping revealed a minimal CC2D1A-CHMP4B binding construct, which includes a short linear sequence within the third DM14 domain of CC2D1A. The CC2D1A binding site on CHMP4B was mapped to the N-terminal helical hairpin. Based on a crystal structure of the CHMP4B helical hairpin, two surface patches were identified that interfere with CC2D1A interaction as determined by surface plasmon resonance. Introducing these mutations into a C-terminal truncation of CHMP4B that exerts a potent dominant negative effect on human immunodeficiency virus type 1 budding revealed that one of the mutants lost this effect completely. This suggests that the identified CC2D1A binding surface might be required for CHMP4B polymerization, which is consistent with the finding that CC2D1A binding to CHMP4B prevents CHMP4B polymerization in vitro. Thus, CC2D1A might act as a negative regulator of CHMP4B function.

PubMed: 22406677
DOI: 10.1016/J.JMB.2012.02.044

実験手法

X-RAY DIFFRACTION (1.8 Å)