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Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo

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作者： Sal-Man N ^[1] ; Shai Y

作者单位： Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel ^[1]

关键词 assembly peptide positively charged residues Tar receptor transmembrane domain LIGAND-BINDING DOMAIN POLAR RESIDUES GLYCOPHORIN-A DIMERIZATION MOTIF ALPHA-HELICES GAMMA-SUBUNIT PI-STACKING PROTEINS SEGMENT MEMBRANE

发布时间 2013-11-20

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The Biochemical Journal

2005年385卷Pt.1期

29-36页

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The Biochemical Journal

2005年385卷Pt.1期

29-36页

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Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo

The Biochemical Journal

相似文献

The Biochemical Journal

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Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo

The Biochemical Journal

相似文献

The Biochemical Journal

相关期刊

检索历史清除