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2efl

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==Crystal structure of the EFC domain of formin-binding protein 17==
==Crystal structure of the EFC domain of formin-binding protein 17==
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<StructureSection load='2efl' size='340' side='right' caption='[[2efl]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
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<StructureSection load='2efl' size='340' side='right'caption='[[2efl]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2efl]] 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=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2efl]] 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=2EFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.61&#8491;</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://pdbe.org/2efl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2efl ProSAT], [http://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [https://pdbe.org/2efl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [https://www.ebi.ac.uk/pdbsum/2efl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2efl ProSAT], [https://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
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[https://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:15252009</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref> <ref>PMID:16418535</ref> <ref>PMID:17512409</ref>
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[https://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:15252009</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref> <ref>PMID:16418535</ref> <ref>PMID:17512409</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Niwa, H]]
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[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Niwa H]]
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[[Category: Shimada, A]]
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[[Category: Shimada A]]
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[[Category: Shirouzu, M]]
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[[Category: Shirouzu M]]
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[[Category: Terada, T]]
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[[Category: Terada T]]
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[[Category: Yokoyama, S]]
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[[Category: Yokoyama S]]
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[[Category: Efc domain]]
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[[Category: Endocytosis-exocytosis complex]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Rsgi]]
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Current revision

Crystal structure of the EFC domain of formin-binding protein 17

PDB ID 2efl

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