5AMO

Structure of a mouse Olfactomedin-1 disulfide-linked dimer of the Olfactomedin domain and part of the coiled coil

5AMO の概要

• エントリーDOI: 10.2210/pdb5amo/pdb
• 分子名称: NOELIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: signaling protein, olfm1, disulfide, neurobiology, development, ampa receptor, beta propeller
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 110603.00

構造登録者

Pronker, M.F.,Bos, T.G.A.A.,Sharp, T.H.,Thies-Weesie, D.M.,Janssen, B.J.C. (登録日: 2015-03-11, 公開日: 2015-04-29, 最終更新日: 2024-11-13)

主引用文献

Pronker, M.F.,Bos, T.G.A.A.,Sharp, T.H.,Thies-Weesie, D.M.,Janssen, B.J.C.
Olfactomedin-1 Has a V-Shaped Disulfide-Linked Tetrameric Structure.
J.Biol.Chem., 290:15092-, 2015

PubMed Abstract: Olfactomedin-1 (Olfm1; also known as noelin and pancortin) is a member of the olfactomedin domain-containing superfamily and a highly expressed neuronal glycoprotein important for nervous system development. It binds a number of secreted proteins and cell surface-bound receptors to induce cell signaling processes. Using a combined approach of x-ray crystallography, solution scattering, analytical ultracentrifugation, and electron microscopy we determined that full-length Olfm1 forms disulfide-linked tetramers with a distinctive V-shaped architecture. The base of the "V" is formed by two disulfide-linked dimeric N-terminal domains. Each of the two V legs consists of a parallel dimeric disulfide-linked coiled coil with a C-terminal β-propeller dimer at the tips. This agrees with our crystal structure of a C-terminal coiled-coil segment and β-propeller combination (Olfm1(coil-Olf)) that reveals a disulfide-linked dimeric arrangement with the β-propeller top faces in an outward exposed orientation. Similar to its family member myocilin, Olfm1 is stabilized by calcium. The dimer-of-dimers architecture suggests a role for Olfm1 in clustering receptors to regulate signaling and sheds light on the conformation of several other olfactomedin domain family members.

PubMed: 25903135
DOI: 10.1074/JBC.M115.653485

実験手法

X-RAY DIFFRACTION (2.4 Å)