1WR0

Structural characterization of the MIT domain from human Vps4b

1WR0 の概要

• エントリーDOI: 10.2210/pdb1wr0/pdb
• 分子名称: SKD1 protein (1 entity in total)
• 機能のキーワード: vps4b, skd1, mit domain, escort, mvb, snps, protein transport, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Prevacuolar compartment membrane; Peripheral membrane protein: O75351
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9207.31

構造登録者

Takasu, H.,Jee, J.G.,Ohno, A.,Goda, N.,Fujiwara, K.,Tochio, H.,Shirakawa, M.,Hiroaki, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-10-07, 公開日: 2005-08-02, 最終更新日: 2024-05-29)

主引用文献

Takasu, H.,Jee, J.G.,Ohno, A.,Goda, N.,Fujiwara, K.,Tochio, H.,Shirakawa, M.,Hiroaki, H.
Structural characterization of the MIT domain from human Vps4b
Biochem.Biophys.Res.Commun., 334:460-465, 2005

PubMed Abstract: The microtubule interacting and trafficking (MIT) domain is a small protein module of unknown function that is conserved in proteins of diverse function, such as Vps4, sorting nexin 15 (SNX15), and spastin. One non-synonymous single nucleotide polymorphism was reported, which results in a Ile58-to-Met (I58M) substitution in hVps4b. Here, we have determined the solution structure of the MIT domain isolated from the NH(2)-terminus of human Vps4b, an AAA-ATPase involved in multivesicular body formation. The MIT domain adopts an 'up-and-down' three-helix bundle. Comparison with the sequences of other MIT domains clearly shows that the residues involved in inter-helical contacts are well conserved. The Ile58-to-Met substitution resulted a substantial thermal instability. In addition, we found a shallow crevice between helices A and C that may serve as a protein-binding site. We propose that the MIT domain serves as a putative adaptor domain for the ESCRT-III complex involved in endosomal trafficking.

PubMed: 16018968
DOI: 10.1016/j.bbrc.2005.06.110

実験手法

SOLUTION NMR