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| | ==Holo form of Calmodulin-Like Domain of Human Non-Muscle alpha-actinin 1== | | ==Holo form of Calmodulin-Like Domain of Human Non-Muscle alpha-actinin 1== |
| - | <StructureSection load='2n8y' size='340' side='right' caption='[[2n8y]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2n8y' size='340' side='right'caption='[[2n8y]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n8y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N8Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n8y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N8Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2n8z|2n8z]]</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=2n8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n8y OCA], [https://pdbe.org/2n8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n8y RCSB], [https://www.ebi.ac.uk/pdbsum/2n8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n8y ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACTN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n8y OCA], [http://pdbe.org/2n8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n8y RCSB], [http://www.ebi.ac.uk/pdbsum/2n8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n8y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACTN1_HUMAN ACTN1_HUMAN]] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. | + | [https://www.uniprot.org/uniprot/ACTN1_HUMAN ACTN1_HUMAN] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Actinin|Actinin]] | + | *[[Actinin 3D structures|Actinin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Backman, L]] | + | [[Category: Large Structures]] |
| - | [[Category: Djinovic-Carugo, K]] | + | [[Category: Backman L]] |
| - | [[Category: Hartl, M]] | + | [[Category: Djinovic-Carugo K]] |
| - | [[Category: Ilc, G]] | + | [[Category: Drmota Prebil S]] |
| - | [[Category: Lenarcic, B]] | + | [[Category: Hartl M]] |
| - | [[Category: Pavsic, M]] | + | [[Category: Ilc G]] |
| - | [[Category: Plavec, J]] | + | [[Category: Lenarcic B]] |
| - | [[Category: Prebil, S Drmota]]
| + | [[Category: Pavsic M]] |
| - | [[Category: Ribeiro, E de Almeida]]
| + | [[Category: Plavec J]] |
| - | [[Category: Slapsak, U]] | + | [[Category: Slapsak U]] |
| - | [[Category: Zielinska, K]] | + | [[Category: Zielinska K]] |
| - | [[Category: Calcium binding protein]] | + | [[Category: De Almeida Ribeiro E]] |
| Structural highlights
Function
ACTN1_HUMAN F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
Publication Abstract from PubMed
The activity of several cytosolic proteins critically depends on the concentration of calcium ions. One important intracellular calcium-sensing protein is alpha-actinin-1, the major actin crosslinking protein in focal adhesions and stress fibers. The actin crosslinking activity of alpha-actinin-1 has been proposed to be negatively regulated by calcium, but the underlying molecular mechanisms are poorly understood. To address this, we determined the first high-resolution NMR structure of its functional calmodulin-like domain (CaMD) in calcium-bound and calcium-free form. These structures reveal that in the absence of calcium, CaMD displays a conformationally flexible ensemble that undergoes a structural change upon calcium binding, leading to limited rotation of the N- and C-terminal lobes around the connecting linker and consequent stabilization of the calcium-loaded structure. Mutagenesis experiments, coupled with mass-spectrometry and isothermal calorimetry data designed to validate the calcium binding stoichiometry and binding site, showed that human non-muscle alpha-actinin-1 binds a single calcium ion within the N-terminal lobe. Finally, based on our structural data and analogy with other alpha-actinins, we provide a structural model of regulation of the actin crosslinking activity of alpha-actinin-1 where calcium induced structural stabilisation causes fastening of the juxtaposed actin binding domain, leading to impaired capacity to crosslink actin.
Structure and calcium-binding studies of calmodulin-like domain of human non-muscle alpha-actinin-1.,Drmota Prebil S, Slapsak U, Pavsic M, Ilc G, Puz V, de Almeida Ribeiro E, Anrather D, Hartl M, Backman L, Plavec J, Lenarcic B, Djinovic-Carugo K Sci Rep. 2016 Jun 7;6:27383. doi: 10.1038/srep27383. PMID:27272015[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Drmota Prebil S, Slapsak U, Pavsic M, Ilc G, Puz V, de Almeida Ribeiro E, Anrather D, Hartl M, Backman L, Plavec J, Lenarcic B, Djinovic-Carugo K. Structure and calcium-binding studies of calmodulin-like domain of human non-muscle alpha-actinin-1. Sci Rep. 2016 Jun 7;6:27383. doi: 10.1038/srep27383. PMID:27272015 doi:http://dx.doi.org/10.1038/srep27383
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