5hzi
From Proteopedia
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==Crystal structure of photoinhibitable Intersectin1 containing C450M mutant LOV2 domain== | ==Crystal structure of photoinhibitable Intersectin1 containing C450M mutant LOV2 domain== | ||
| - | <StructureSection load='5hzi' size='340' side='right' caption='[[5hzi]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='5hzi' size='340' side='right'caption='[[5hzi]], [[Resolution|resolution]] 2.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5hzi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HZI OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5hzi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Avena_sativa Avena sativa] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HZI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 2.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=5hzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hzi OCA], [https://pdbe.org/5hzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hzi RCSB], [https://www.ebi.ac.uk/pdbsum/5hzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hzi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ITSN1_HUMAN ITSN1_HUMAN] Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2. Isoform 1 could be involved in brain-specific synaptic vesicle recycling. Inhibits ARHGAP31 activity toward RAC1.<ref>PMID:11744688</ref> <ref>PMID:22648170</ref> [https://www.uniprot.org/uniprot/O49003_AVESA O49003_AVESA] |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Optogenetic and chemogenetic control of proteins has revealed otherwise inaccessible facets of signaling dynamics. Here, we use light- or ligand-sensitive domains to modulate the structural disorder of diverse proteins, thereby generating robust allosteric switches. Sensory domains were inserted into nonconserved, surface-exposed loops that were tight and identified computationally as allosterically coupled to active sites. Allosteric switches introduced into motility signaling proteins (kinases, guanosine triphosphatases, and guanine exchange factors) controlled conversion between conformations closely resembling natural active and inactive states, as well as modulated the morphodynamics of living cells. Our results illustrate a broadly applicable approach to design physiological protein switches. | ||
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| + | Engineering extrinsic disorder to control protein activity in living cells.,Dagliyan O, Tarnawski M, Chu PH, Shirvanyants D, Schlichting I, Dokholyan NV, Hahn KM Science. 2016 Dec 16;354(6318):1441-1444. PMID:27980211<ref>PMID:27980211</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5hzi" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Avena sativa]] |
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Chu PH]] |
| - | [[Category: | + | [[Category: Dagliyan O]] |
| - | [[Category: | + | [[Category: Dokholyan NV]] |
| - | [[Category: | + | [[Category: Hahn KM]] |
| - | [[Category: | + | [[Category: Schlichting I]] |
| - | [[Category: | + | [[Category: Shirvanyants D]] |
| - | [[Category: | + | [[Category: Tarnawski M]] |
Current revision
Crystal structure of photoinhibitable Intersectin1 containing C450M mutant LOV2 domain
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