|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution NMR structure of titin N2A region Ig domain I83== | | ==Solution NMR structure of titin N2A region Ig domain I83== |
| - | <StructureSection load='6yj0' size='340' side='right'caption='[[6yj0]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''> | + | <StructureSection load='6yj0' size='340' side='right'caption='[[6yj0]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6yj0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YJ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yj0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YJ0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ttn ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6yj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yj0 OCA], [https://pdbe.org/6yj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yj0 RCSB], [https://www.ebi.ac.uk/pdbsum/6yj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yj0 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6yj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yj0 OCA], [https://pdbe.org/6yj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yj0 RCSB], [https://www.ebi.ac.uk/pdbsum/6yj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yj0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TITIN_MOUSE TITIN_MOUSE]] 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.[UniProtKB:Q8WZ42]<ref>PMID:16702235</ref> <ref>PMID:17261657</ref>
| + | [https://www.uniprot.org/uniprot/TITIN_MOUSE TITIN_MOUSE] 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.[UniProtKB:Q8WZ42]<ref>PMID:16702235</ref> <ref>PMID:17261657</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 19: |
Line 17: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6yj0" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6yj0" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Titin 3D structures|Titin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 24: |
Line 25: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Gage M]] |
| - | [[Category: Gage, M]] | + | [[Category: Pfuhl M]] |
| - | [[Category: Pfuhl, M]] | + | |
| - | [[Category: Calcium binding actin binding muscle i-band]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
TITIN_MOUSE 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.[UniProtKB:Q8WZ42][1] [2]
Publication Abstract from PubMed
Titin, the largest single chain protein known so far, has long been known to play a critical role in passive muscle function but recent studies have highlighted titin's role in active muscle function. One of the key elements in this role is the Ca(2+)-dependent interaction between titin's N2A region and the thin filament. An important element in this interaction is I83, the terminal immunoglobulin domain in the N2A region. There is limited structural information about this domain, but experimental evidence suggests that it plays a critical role in the N2A-actin binding interaction. We now report the solution NMR structure of I83 and characterize its dynamics and metal binding properties in detail. Its structure shows interesting relationships to other I-band Ig domains. Metal binding and dynamics data point towards the way the domain is evolutionarily optimized to interact with neighbouring domains. We also identify a calcium binding site on the N-terminal side of I83, which is expected to impact the interdomain interaction with the I82 domain. Together these results provide a first step towards a better understanding of the physiological effects associated with deletion of most of the I83 domain, as occurs in the mdm mouse model, as well as for future investigations of the N2A region.
Solution NMR structure of titin N2A region Ig domain I83 and its interaction with metal ions.,Kelly C, Pace N, Gage M, Pfuhl M J Mol Biol. 2021 Mar 31:166977. doi: 10.1016/j.jmb.2021.166977. PMID:33811919[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weinert S, Bergmann N, Luo X, Erdmann B, Gotthardt M. M line-deficient titin causes cardiac lethality through impaired maturation of the sarcomere. J Cell Biol. 2006 May 22;173(4):559-70. Epub 2006 May 15. PMID:16702235 doi:http://dx.doi.org/jcb.200601014
- ↑ Peng J, Raddatz K, Molkentin JD, Wu Y, Labeit S, Granzier H, Gotthardt M. Cardiac hypertrophy and reduced contractility in hearts deficient in the titin kinase region. Circulation. 2007 Feb 13;115(6):743-51. doi: 10.1161/CIRCULATIONAHA.106.645499., Epub 2007 Jan 29. PMID:17261657 doi:http://dx.doi.org/10.1161/CIRCULATIONAHA.106.645499
- ↑ Kelly C, Pace N, Gage M, Pfuhl M. Solution NMR structure of titin N2A region Ig domain I83 and its interaction with metal ions. J Mol Biol. 2021 Mar 31:166977. doi: 10.1016/j.jmb.2021.166977. PMID:33811919 doi:http://dx.doi.org/10.1016/j.jmb.2021.166977
|
