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| Content Provider | Springer Nature Link |
|---|---|
| Author | Tossavainen, Helena Seppälä, Jonne Sethi, Ritika Pihlajamaa, Tero Permi, Perttu |
| Copyright Year | 2014 |
| Abstract | Filamins regulate the actin cytoskeleton by cross-linking actin filaments, linking the cytoskeleton to the cell membrane, and through interaction with numerous binding partners such as intracellular signalling molecules, ion channels, receptors, enzymes and transcription factors. The rod region of filamins consists of 24 immunoglubulin (Ig)-like repeats, for some of which the functional unit is a domain pair. Our aim is to study filamin Ig domain–domain interactions and quaternary arrangement as well as to locate peptide binding sites on domain assemblies. We report here the H$^{N}$, N$^{H}$, C$^{α}$, C$^{β}$, and methyl group assignments of filamin A three-domain fragment IgFLNa3–5 and filamin C two-domain fragment IgFLNc4–5. |
| Starting Page | 47 |
| Ending Page | 50 |
| Page Count | 4 |
| File Format | |
| ISSN | 18742718 |
| Journal | Biomolecular NMR Assignments |
| Volume Number | 9 |
| Issue Number | 1 |
| e-ISSN | 1874270X |
| Language | English |
| Publisher | Springer Netherlands |
| Publisher Date | 2014-01-11 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Domain arrangement Filamin NMR Resonance assignment Biophysics and Biological Physics Polymer Sciences Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Biochemistry |
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