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2efl
From Proteopedia
(Difference between revisions)
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<StructureSection load='2efl' size='340' side='right'caption='[[2efl]], [[Resolution|resolution]] 2.61Å' scene=''> | <StructureSection load='2efl' size='340' side='right'caption='[[2efl]], [[Resolution|resolution]] 2.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2EFL FirstGlance]. <br> |
</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> | </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> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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 == | ||
| - | [[ | + | [[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 == | ||
| - | [[ | + | [[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]] | ||
Revision as of 17:23, 15 December 2021
Crystal structure of the EFC domain of formin-binding protein 17
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