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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TITIN_HUMAN TITIN_HUMAN]] Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.<ref>PMID:9804419</ref> | [[http://www.uniprot.org/uniprot/TITIN_HUMAN TITIN_HUMAN]] Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.<ref>PMID:9804419</ref> | ||
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== Publication Abstract from PubMed == | |||
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. | |||
Structural Insights on the Obscurin-Binding Domains in Titin.,Letourneau AG, Wright NT Protein Pept Lett. 2018;25(11):973-979. doi: 10.2174/0929866525666181004102031. PMID:30289063<ref>PMID:30289063</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | |||
*[[Titin|Titin]] | |||
== References == | == References == | ||
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