1P23

STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION, NMR, 10 STRUCTURES

1P23 の概要

• エントリーDOI: 10.2210/pdb1p23/pdb
• 分子名称: TRANSMEMBRANE PROTEIN TMP21 PRECURSOR (1 entity in total)
• 機能のキーワード: transport, protein transport, transmembrane, glycoprotein, vesicular transport, cop, coatomer, golgi stack, solution structure, p24 family, integral membrane protein, membrane protein
• 細胞内の位置: Golgi apparatus membrane; Single-pass type I membrane protein; Lumenal side: Q28735
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 7281.08

構造登録者

Weidler, M.,Reinhard, C.,Wieland, F.T.,Roesch, P. (登録日: 1998-11-17, 公開日: 2000-06-07, 最終更新日: 2024-10-30)

主引用文献

Weidler, M.,Reinhard, C.,Friedrich, G.,Wieland, F.T.,Rosch, P.
Structure of the cytoplasmic domain of p23 in solution: implications for the formation of COPI vesicles.
Biochem.Biophys.Res.Commun., 271:401-408, 2000

PubMed Abstract: Coatomer, the coat protein complex of coat protein (COPI) vesicles, is involved in the budding of these vesicles. Its interaction with the cytoplasmic domains of some p24-family members, type I transmembrane proteins of the Golgi, has been shown to induce a conformational change of coatomer that initiates polymerization of the complex. From stoichiometrical data it is likely that interaction of coatomer with the small tail domains involves an oligomeric form of the p24 proteins. Here we present the structure of peptide analogs of the cytoplasmic domain of p23, a member of the p24 family, as determined by two-dimensional nuclear magnetic resonance spectroscopy in the presence of 2,2,2-trifluoroethanol. An improved strategy for structure calculation revealed that the tail domain peptides form alpha-helices and adopt a tetrameric state. Based on these results we propose an initial model for the binding of coatomer by p23 and the induced conformational change of coatomer that results in its polymerization, curvature of the Golgi membrane to form a bud, and finally a COPI-coated vesicle.

PubMed: 10799309
DOI: 10.1006/bbrc.2000.2511

実験手法

SOLUTION NMR