2R51

Crystal Structure of mouse Vps26B

2R51 の概要

• エントリーDOI: 10.2210/pdb2r51/pdb
• 分子名称: Vacuolar protein sorting-associated protein 26B (2 entities in total)
• 機能のキーワード: retromer, fibronectin iii, arrestin domain, membrane, phosphorylation, protein transport, transport, transport protein
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cytoplasm: Q8C0E2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40078.29

構造登録者

Owen, D.J.,Teasdale, R.D.,Collins, B.M. (登録日: 2007-09-02, 公開日: 2008-07-15, 最終更新日: 2024-10-30)

主引用文献

Collins, B.M.,Norwood, S.J.,Kerr, M.C.,Mahony, D.,Seaman, M.N.,Teasdale, R.D.,Owen, D.J.
Structure of Vps26B and mapping of its interaction with the retromer protein complex.
Traffic, 9:366-379, 2008

PubMed Abstract: Retromer is a heteromeric protein complex with important roles in endosomal membrane trafficking, most notably in the retrograde transport of lysosomal hydrolase receptors from endosomes to the Golgi. The core of retromer is composed of three subunits vacuolar protein sorting (Vps)35, Vps26 and Vps29, and in mammals, there are two paralogues of the medium subunit Vps26A and Vps26B. We find that both Vps26A and Vps26B bind to Vps35/Vps29 with nanomolar affinity and compete for a single-binding site to define distinct retromer complexes in vitro and in vivo. We have determined the crystal structure of mouse Vps26B and compare this structure with that of Vps26A. Vps26 proteins have a striking similarity to the arrestin family of proteins that regulate the signalling and endocytosis of G-protein-coupled receptors, although we observe that surface residues involved in arrestin function are not conserved in Vps26. Using structure-based mutagenesis, we show that both Vps26A and Vps26B are incorporated into retromer complexes through binding of Vps35 to a highly conserved surface patch within the C-terminal subdomain and that this interaction is required for endosomal recruitment of the proteins.

PubMed: 18088321
DOI: 10.1111/j.1600-0854.2007.00688.x

実験手法

X-RAY DIFFRACTION (2.1 Å)