Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection

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• 作者：Stefano Pernigo¹ ; Atsushi Fukuzawa¹ ; ² ; Amy E.M. Beedle¹ ; ³ ; Mark Holt¹ ; ² ; Adam Round⁴ ; ⁶ ; ⁷ ; Alessandro Pandini¹ ; ⁵ ; Sergi Garcia-Manyes¹ ; ³ ; ^{sergi.garcia-manyes@kcl.ac.uk} ; Mathias Gautel¹ ; ² ; ^{mathias.gautel@kcl.ac.uk} ; Roberto A. Steiner¹ ; ⁸ ; ^{roberto.steiner@kcl.ac.uk}
• 关键词：muscle ; M-band ; myomesin ; obscurin ; obscurin-like-1 ; protein complexes ; X-ray crystallography ; SAXS ; atomic force microscopy ; immunoglobulin domain
• 刊名：Structure
• 出版年：2017
• 出版时间：3 January 2017
• 年：2017
• 卷：25
• 期：1
• 页码：107-120
• 全文大小：4950 K
• 卷排序：25

文摘

The structure of the human obscurin-like-1:myomesin complex has been determined A myomesin sequence complements an immunoglobulin fold of obscurin-like-1 This binding mechanism provides mechanical stability up to forces of ∼135 pN Possible implications on muscle nanomechanics and M-band organization are discussed