|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1vf6' size='340' side='right'caption='[[1vf6]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1vf6' size='340' side='right'caption='[[1vf6]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1vf6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VF6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1vf6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VF6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rso|1rso]]</div></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]] 2.1Å</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=1vf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vf6 OCA], [https://pdbe.org/1vf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vf6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vf6 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=1vf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vf6 OCA], [https://pdbe.org/1vf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vf6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vf6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/INADL_HUMAN INADL_HUMAN]] Scaffolding protein that may bring different proteins into adjacent positions at the cell membrane. May regulate protein targeting, cell polarity and integrity of tight junctions. May regulate the surface expression and/or function of ASIC3 in sensory neurons.<ref>PMID:11927608</ref> [[https://www.uniprot.org/uniprot/MPP5_MOUSE MPP5_MOUSE]] May play a role in tight junctions biogenesis and in the establishment of cell polarity in epithelial cells. May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter. Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton.<ref>PMID:15677456</ref>
| + | [https://www.uniprot.org/uniprot/INADL_HUMAN INADL_HUMAN] Scaffolding protein that may bring different proteins into adjacent positions at the cell membrane. May regulate protein targeting, cell polarity and integrity of tight junctions. May regulate the surface expression and/or function of ASIC3 in sensory neurons.<ref>PMID:11927608</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Karnak, D]] | + | [[Category: Karnak D]] |
| - | [[Category: Lavie, A]] | + | [[Category: Lavie A]] |
| - | [[Category: Li, Y]] | + | [[Category: Li Y]] |
| - | [[Category: Margolis, B]] | + | [[Category: Margolis B]] |
| - | [[Category: Coiled-coil]]
| + | |
| - | [[Category: Four-helical bundle]]
| + | |
| - | [[Category: Heterodimer]]
| + | |
| - | [[Category: Hydrophobic packing interaction]]
| + | |
| - | [[Category: L27 domain]]
| + | |
| - | [[Category: Protein binding-protein transport complex]]
| + | |
| Structural highlights
Function
INADL_HUMAN Scaffolding protein that may bring different proteins into adjacent positions at the cell membrane. May regulate protein targeting, cell polarity and integrity of tight junctions. May regulate the surface expression and/or function of ASIC3 in sensory neurons.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
L27 is a protein-binding domain that can assemble essential proteins for signaling and cell polarity into complexes by interacting in a heterodimeric manner. One of these protein complexes is the PATJ/PALS1/Crumbs tripartite complex, which is crucial for the establishment and maintenance of cell polarity. To reveal the structural basis underlining the obligate heterodimerization, we have determined the crystal structure of the PALS1-L27N/PATJ-L27 heterodimer complex. Each L27 domain is composed of three helices. The two L27 domains heterodimerize by building a compact structure consisting of a four-helix bundle formed by the first two helices of each L27 domain and one coiled-coil formed by the third helix of each domain. The large hydrophobic packing interactions contributed by all the helices of both L27 domains predominantly drive the heterodimer formation, which is likely to be a general feature of L27 domains. Combined with mutational studies, we can begin to understand the structural basis for the specificity of L27 binding pairs. Our results provide unique insights into L27 domain heterodimer complex, which is critical for cell polarization.
Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes.,Li Y, Karnak D, Demeler B, Margolis B, Lavie A EMBO J. 2004 Jul 21;23(14):2723-33. Epub 2004 Jul 8. PMID:15241471[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roh MH, Makarova O, Liu CJ, Shin K, Lee S, Laurinec S, Goyal M, Wiggins R, Margolis B. The Maguk protein, Pals1, functions as an adapter, linking mammalian homologues of Crumbs and Discs Lost. J Cell Biol. 2002 Apr 1;157(1):161-72. Epub 2002 Apr 1. PMID:11927608 doi:http://dx.doi.org/10.1083/jcb.200109010
- ↑ Li Y, Karnak D, Demeler B, Margolis B, Lavie A. Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes. EMBO J. 2004 Jul 21;23(14):2723-33. Epub 2004 Jul 8. PMID:15241471 doi:10.1038/sj.emboj.7600294
|
