ArticleJournal of muscle research and cell motility2005
Poly-Ig tandems from I-band titin share extended domain arrangements irrespective of the distinct features of their modular constituents.
Article in Journal of muscle research and cell motility, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
- Nx3 Is a Z-Disk Structural and Signaling Hub That Is Reduced in Heart Failure.Circulation research · 2026Article
- Mechanically weak and highly dynamic state of mechanosensitive titin Ig domains induced by proline isomerization.Nature communications · 2025Article
- Molecular insights into titin's A-band.Journal of muscle research and cell motility · 2023Article
- Immunological and Structural Characterization of Titin Main Immunogenic Region; I110 Domain Is the Target of Titin Antibodies in Myasthenia Gravis.Biomedicines · 2023Article
- Pairwise sequence similarity mapping with PaSiMap: Reclassification of immunoglobulin domains from titin as case study.Computational and structural biotechnology journal · 2022Article
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- Titin N2A Domain and Its Interactions at the Sarcomere.International journal of molecular sciences · 2021Review
- The N2A region of titin has a unique structural configuration.The Journal of general physiology · 2021Article
- Solution NMR Structure of Titin N2A Region Ig Domain I83 and Its Interaction with Metal Ions.Journal of molecular biology · 2021Article
- Molecular Characterisation of Titin N2A and Its Binding of CARP Reveals a Titin/Actin Cross-linking Mechanism.Journal of molecular biology · 2021Article
- The Costs of Close Contacts: Visualizing the Energy Landscape of Cell Contacts at the Nanoscale.Biophysical journal · 2020Article
- The ZT Biopolymer: A Self-Assembling Protein Scaffold for Stem Cell Applications.International journal of molecular sciences · 2019Review
- Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment.PloS one · 2019Article
- Conformational plasticity and evolutionary analysis of the myotilin tandem Ig domains.Scientific reports · 2017Article
- Exploration of pathomechanisms triggered by a single-nucleotide polymorphism in titin's I-band: the cardiomyopathy-linked mutation T2580I.Open biology · 2016Article
- Titin and obscurin: giants holding hands and discovery of a new Ig domain subset.Journal of molecular biology · 2015Article
- Structure of giant muscle proteins.Frontiers in physiology · 2013Review
- Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium.European biophysics journal : EBJ · 2013Article
- Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism.The Journal of biological chemistry · 2013Article
- Roles of titin in the structure and elasticity of the sarcomere.Journal of biomedicine & biotechnology · 2010Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cellular function of the giant protein titin in striated muscle is a major focus of scientific attention. Particularly, its role in passive mechanics has been extensively investigated. In strong contrast, the structural details of this filament are very poorly understood. To date, only a handful of atomic models from single domain components have become available and data on poly-constructs are limited to scarce SAXS analyses. In this study, we examine the molecular parameters of poly-Ig tandems from I-band titin relevant to muscle elasticity. We revisit conservation patterns in domain and linker sequences of I-band modules and interpret these in the light of available atomic structures of Ig domains from muscle proteins. The emphasis is placed on features expected to affect inter-domain arrangements. We examine the overall conformation of a 6Ig fragment, I65-I70, from the skeletal I-band of soleus titin using SAXS and electron microscopy approaches. The possible effect of highly conserved glutamate groups at the linkers as well as the ionic strength of the medium on the overall molecular parameters of this sample is investigated. Our findings indicate that poly-Ig tandems from I-band titin tend to adopt extended arrangements with low or moderate intrinsic flexibility, independently of the specific features of linkers or component Ig domains across constitutively- and differentially-expressed tandems. Linkers do not appear to operate as free hinges so that lateral association of Ig domains must occur infrequently in samples in solution, even that inter-domain sequences of 4-5 residues length would well accommodate such geometry. It can be expected that this principle is generally applicable to all Ig-tandems from I-band titin.
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