Binding interactions of the peripheral stalk subunit isoforms from human V-ATPase

The mammalian peripheral stalk subunits of the vacuolar-type H + -ATPases (V-ATPases) possess several isoforms (C1, C2, E1, E2, G1, G2, G3, a1, a2, a3, and a4), which may play significant role in regulating ATPase assembly and disassembly in different tissues. To better understand the structure and...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2016-05, Vol.80 (5), p.878-890
Hauptverfasser:	Rahman, Suhaila, Yamato, Ichiro, Saijo, Shinya, Mizutani, Kenji, Takamuku, Yuuki, Ishizuka-Katsura, Yoshiko, Ohsawa, Noboru, Terada, Takaho, Shirouzu, Mikako, Yokoyama, Shigeyuki, Murata, Takeshi
Format:	Artikel
Sprache:	eng
Schlagworte:	affinity Amino Acid Sequence Binding Sites Cell-Free System - metabolism Cloning, Molecular Escherichia coli - genetics Escherichia coli - metabolism human peripheral stalk Humans Isoenzymes - chemistry Isoenzymes - genetics Isoenzymes - metabolism Models, Molecular Protein Binding Protein Biosynthesis Protein Interaction Domains and Motifs Protein Multimerization Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid subunit isoform surface plasmon resonance V-ATPase Vacuolar Proton-Translocating ATPases - chemistry Vacuolar Proton-Translocating ATPases - genetics Vacuolar Proton-Translocating ATPases - metabolism
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