4BWD

Human short coiled coil protein

4BWD の概要

• エントリーDOI: 10.2210/pdb4bwd/pdb
• 分子名称: SHORT COILED-COIL PROTEIN (2 entities in total)
• 機能のキーワード: structural protein, scaffold protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side: Q9UIL1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 28150.61

構造登録者

Behrens, C.,Binotti, B.,Chua, J.J.,Kuhnel, K. (登録日: 2013-07-01, 公開日: 2013-09-11, 最終更新日: 2024-05-08)

主引用文献

Behrens, C.,Binotti, B.,Schmidt, C.,Robinson, C.V.,Chua, J.J.E.,Kuhnel, K.
Crystal Structure of the Human Short Coiled Coil Protein and Insights Into Scoc-Fez1 Complex Formation.
Plos One, 8:76355-, 2013

PubMed Abstract: The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta 1 (FEZ1). This complex is involved in autophagy regulation. We determined the crystal structure of the coiled coil domain of human SCOC at 2.7 Å resolution. SCOC forms a parallel left handed coiled coil dimer. We observed two distinct dimers in the crystal structure, which shows that SCOC is conformationally flexible. This plasticity is due to the high incidence of polar and charged residues at the core a/d-heptad positions. We prepared two double mutants, where these core residues were mutated to either leucines or valines (E93V/K97L and N125L/N132V). These mutations led to a dramatic increase in stability and change of oligomerisation state. The oligomerisation state of the mutants was characterized by multi-angle laser light scattering and native mass spectrometry measurements. The E93V/K97 mutant forms a trimer and the N125L/N132V mutant is a tetramer. We further demonstrate that SCOC forms a stable homogeneous complex with the coiled coil domain of FEZ1. SCOC dimerization and the SCOC surface residue R117 are important for this interaction.

PubMed: 24098481
DOI: 10.1371/JOURNAL.PONE.0076355

実験手法

X-RAY DIFFRACTION (2.702 Å)