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Title: Structural Insights on the Obscurin-Binding Domains in Titin. Author: Letourneau AG, Wright NT. Journal: Protein Pept Lett; 2018; 25(11):973-979. PubMed ID: 30289063. Abstract: INTRODUCTION: The giant muscular proteins titin and obscurin bind to each other at the Zdisk during muscle development. This binding event is mediated through two domains from each protein: ZIg9/10 from titin and Ig58/59 from obscurin. This interaction helps stabilize and organize the sarcomere; ablation of this binding leads to muscular dystrophy. OBJECTIVE: Here we solve the high-resolution solution structure of titin ZIg10 and further delineate which sections of titin bind to obscurin. MATERIALS AND METHODS: Solution NMR, Circular Dichroism, and SEC-MALS were used to biophysically characterize the titin domains involved in this titin-obscurin interaction. RESULTS AND CONCLUSION: We present the high-resolution solution structure of titin ZIg10. Additionally, we show that titin ZIg9 drives the titin-obscurin interaction, while ZIg10 does not actively participate in the titin-obscurin interaction but instead acts to stabilize ZIg9.[Abstract] [Full Text] [Related] [New Search]