1t2l
From Proteopedia
(Difference between revisions)
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<StructureSection load='1t2l' size='340' side='right'caption='[[1t2l]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1t2l' size='340' side='right'caption='[[1t2l]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1t2l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1t2l]] is a 2 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=1T2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T2L FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1t2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2l OCA], [https://pdbe.org/1t2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t2l RCSB], [https://www.ebi.ac.uk/pdbsum/1t2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2l 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=1t2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2l OCA], [https://pdbe.org/1t2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t2l RCSB], [https://www.ebi.ac.uk/pdbsum/1t2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/COTL1_HUMAN COTL1_HUMAN] Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.<ref>PMID:11583571</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t2l ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t2l ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Human coactosin-like protein is an actin filament binding protein but does not bind to globular actin. It associates with 5-Lipoxygenase both in vivo and in vitro, playing important roles in modulating the activities of actin and 5-Lipoxygenase. Coactosin counteracts the capping activity of capping protein which inhibits the actin polymerization. We determined the crystal structures of human coactosin-like protein by multi-wavelength anomalous dispersion method. The structure showed a high level of similarity to ADF-H domain, although their amino acid sequences share low degree of homology. A few conserved hydrophobic residues that may contribute to the folding were identified. This structure suggests coactosin-like protein bind to F-actin in a different way from ADF/Cofilin family. Combined with the information from previous mutagenesis studies, the binding sites for F-actin and 5-Lipoxygenase were analyzed, respectively. These two sites are quite close, which might prevent F-actin and 5-Lipoxygenase from binding to coactosin simultaneously. | ||
- | |||
- | Crystal structure of human coactosin-like protein.,Liu L, Wei Z, Wang Y, Wan M, Cheng Z, Gong W J Mol Biol. 2004 Nov 19;344(2):317-23. PMID:15522287<ref>PMID:15522287</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1t2l" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Chen | + | [[Category: Chen Z]] |
- | [[Category: Gong | + | [[Category: Gong W]] |
- | [[Category: Liu | + | [[Category: Liu L]] |
- | [[Category: Wang | + | [[Category: Wang Y]] |
- | [[Category: Wei | + | [[Category: Wei Z]] |
- | + | ||
- | + |
Revision as of 08:37, 1 May 2024
Three Crystal Structures of Human Coactosin-like Protein
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Categories: Homo sapiens | Large Structures | Chen Z | Gong W | Liu L | Wang Y | Wei Z