2n8y: Difference between revisions

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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 [https://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 [https://proteopedia.org/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" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[2n8z|2n8z]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACTN1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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 ==
Line 27: Line 25:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Backman, L]]
[[Category: Backman L]]
[[Category: Djinovic-Carugo, K]]
[[Category: Djinovic-Carugo K]]
[[Category: Hartl, M]]
[[Category: Drmota Prebil S]]
[[Category: Ilc, G]]
[[Category: Hartl M]]
[[Category: Lenarcic, B]]
[[Category: Ilc G]]
[[Category: Pavsic, M]]
[[Category: Lenarcic B]]
[[Category: Plavec, J]]
[[Category: Pavsic M]]
[[Category: Prebil, S Drmota]]
[[Category: Plavec J]]
[[Category: Ribeiro, E de Almeida]]
[[Category: Slapsak U]]
[[Category: Slapsak, U]]
[[Category: Zielinska K]]
[[Category: Zielinska, K]]
[[Category: De Almeida Ribeiro E]]
[[Category: Calcium binding protein]]

Latest revision as of 13:23, 15 March 2023

Holo form of Calmodulin-Like Domain of Human Non-Muscle alpha-actinin 1Holo form of Calmodulin-Like Domain of Human Non-Muscle alpha-actinin 1

Structural highlights

2n8y is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  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. 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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