The characterization of a novel S100A1 binding site in the N-terminus of TRPM1
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- 作者：Michaela Jirkua ; Zdenek Lanskyb ; Lucie Bednarovac ; Miroslav Sulcd ; e ; Lenka Monincovac ; Pavel Majerc ; Ladislav Vyklickya ; Jiri Vondrasekc ; Jan Teisingera ; Kristyna Bousovaa ; c ; kristyna.bousova@fgu.cas.cz" class="auth_mail" title="E-mail the corresponding author
- 关键词：TRPM1 channel ; Binding site ; Calcium-binding protein S100A1 ; Steady-state fluorescence anisotropy ; Molecular modeling ; Circular dichroism
- 刊名：International Journal of Biochemistry and Cell Biology
- 出版年：2016
- 出版时间：September 2016
- 年：2016
- 卷：78
- 期：Complete
- 页码：186-193
- 全文大小：1991 K
文摘
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TRPM1 N-terminus binds calcium binding protein S100A1.
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Formation of TRPM1/S100A1 complex is facilitated through interactions of clusters positively charged (K271A, R273A, R274A) and hydrophobic (L263A, V270A, L276A) residues.
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TRPM1 N-terminal domain distinctly does not change the secondary structure content upon S100A1 binding.
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Molecular model describes potential molecular mechanism of TRPM1/S100A1 complex formation.