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| | ==Crystal Structure of the coiled-coil, RA and PH domains of Lamellipodin== | | ==Crystal Structure of the coiled-coil, RA and PH domains of Lamellipodin== |
| - | <StructureSection load='4gmv' size='340' side='right' caption='[[4gmv]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4gmv' size='340' side='right'caption='[[4gmv]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gmv]] is a 2 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=4GMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GMV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gmv]] 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=4GMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GMV FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gn1|4gn1]]</td></tr> | + | </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=4gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gmv OCA], [https://pdbe.org/4gmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gmv RCSB], [https://www.ebi.ac.uk/pdbsum/4gmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gmv ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAPH1, ALS2CR18, ALS2CR9, KIAA1681, LPD, PREL2, RMO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gmv OCA], [http://pdbe.org/4gmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gmv RCSB], [http://www.ebi.ac.uk/pdbsum/4gmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gmv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RAPH1_HUMAN RAPH1_HUMAN]] Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion. | + | [https://www.uniprot.org/uniprot/RAPH1_HUMAN RAPH1_HUMAN] Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Chang, Y C.E]] | + | [[Category: Large Structures]] |
| - | [[Category: Wu, J]] | + | [[Category: Chang YCE]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Wu J]] |
| - | [[Category: Cell migration]]
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| - | [[Category: Coiled-coil region]]
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| - | [[Category: Cytoskeletal protein]]
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| - | [[Category: Ena/vasp binding]]
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| - | [[Category: Pleckstrin homology domain]]
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| - | [[Category: Ra-ph]]
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| - | [[Category: Ras-association domain]]
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| Structural highlights
Function
RAPH1_HUMAN Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
Publication Abstract from PubMed
The adapter protein Lamellipodin (Lpd) plays an important role in cell migration. In particular, Lpd mediates lamellipodia formation by regulating actin dynamics via interacting with Ena/VASP proteins. Its RA-PH tandem domain configuration suggests that like its paralog RIAM, Lpd may also mediate particular Ras GTPase signaling. We determined the crystal structures of the Lpd RA-PH domains alone and with an N-terminal coiled-coil region (cc-RA-PH). These structures reveal that apart from the anticipated coiled-coil interaction, Lpd may also oligomerize through a second intermolecular contact site. We then validated both oligomerization interfaces in solution by mutagenesis. A fluorescence-polarization study demonstrated that Lpd binds phosphoinositol with low affinity. Based on our crystallographic and biochemical data, we propose that Lpd and RIAM serve diverse functions: Lpd plays a predominant role in regulating actin polymerization, and its function in mediating Ras GTPase signaling is largely suppressed compared to RIAM.
Crystal structure of Lamellipodin implicates diverse functions in actin polymerization and Ras signaling.,Chang YC, Zhang H, Brennan ML, Wu J Protein Cell. 2013 Mar;4(3):211-9. doi: 10.1007/s13238-013-2082-5. Epub 2013 Mar , 13. PMID:23483482[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chang YC, Zhang H, Brennan ML, Wu J. Crystal structure of Lamellipodin implicates diverse functions in actin polymerization and Ras signaling. Protein Cell. 2013 Mar;4(3):211-9. doi: 10.1007/s13238-013-2082-5. Epub 2013 Mar , 13. PMID:23483482 doi:http://dx.doi.org/10.1007/s13238-013-2082-5
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