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| | <StructureSection load='4z79' size='340' side='right'caption='[[4z79]], [[Resolution|resolution]] 1.54Å' scene=''> | | <StructureSection load='4z79' size='340' side='right'caption='[[4z79]], [[Resolution|resolution]] 1.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4z79]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z79 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z79 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4z79]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z79 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z8g|4z8g]], [[4z94|4z94]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LMOD1 ([http://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=4z79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z79 OCA], [https://pdbe.org/4z79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z79 RCSB], [https://www.ebi.ac.uk/pdbsum/4z79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z79 ProSAT]</span></td></tr> |
| - | <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=4z79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z79 OCA], [http://pdbe.org/4z79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z79 RCSB], [http://www.ebi.ac.uk/pdbsum/4z79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z79 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LMOD1_HUMAN LMOD1_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boczkowska, M]] | + | [[Category: Boczkowska M]] |
| - | [[Category: Dominguez, R]] | + | [[Category: Dominguez R]] |
| - | [[Category: Rebowski, G]] | + | [[Category: Rebowski G]] |
| - | [[Category: Leiomodin-1 actin binding site 2 abs2 actin nucleator]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
LMOD1_HUMAN
Publication Abstract from PubMed
How proteins sharing a common fold have evolved different functions is a fundamental question in biology. Tropomodulins (Tmods) are prototypical actin filament pointed-end-capping proteins, whereas their homologues, Leiomodins (Lmods), are powerful filament nucleators. We show that Tmods and Lmods do not compete biochemically, and display similar but distinct localization in sarcomeres. Changes along the polypeptide chains of Tmods and Lmods exquisitely adapt their functions for capping versus nucleation. Tmods have alternating tropomyosin (TM)- and actin-binding sites (TMBS1, ABS1, TMBS2 and ABS2). Lmods additionally contain a C-terminal extension featuring an actin-binding WH2 domain. Unexpectedly, the different activities of Tmods and Lmods do not arise from the Lmod-specific extension. Instead, nucleation by Lmods depends on two major adaptations-the loss of pointed-end-capping elements present in Tmods and the specialization of the highly conserved ABS2 for recruitment of two or more actin subunits. The WH2 domain plays only an auxiliary role in nucleation.
How Leiomodin and Tropomodulin use a common fold for different actin assembly functions.,Boczkowska M, Rebowski G, Kremneva E, Lappalainen P, Dominguez R Nat Commun. 2015 Sep 15;6:8314. doi: 10.1038/ncomms9314. PMID:26370058[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boczkowska M, Rebowski G, Kremneva E, Lappalainen P, Dominguez R. How Leiomodin and Tropomodulin use a common fold for different actin assembly functions. Nat Commun. 2015 Sep 15;6:8314. doi: 10.1038/ncomms9314. PMID:26370058 doi:http://dx.doi.org/10.1038/ncomms9314
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