|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6d2k' size='340' side='right'caption='[[6d2k]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='6d2k' size='340' side='right'caption='[[6d2k]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6d2k]] is a 1 chain structure with sequence from [http://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=6D2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D2K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d2k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D2K FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6d21|6d21]]</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]] 1.55Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Farp2, Kiaa0793 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6d2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d2k OCA], [https://pdbe.org/6d2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d2k RCSB], [https://www.ebi.ac.uk/pdbsum/6d2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d2k ProSAT]</span></td></tr> |
| - | <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=6d2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d2k OCA], [http://pdbe.org/6d2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d2k RCSB], [http://www.ebi.ac.uk/pdbsum/6d2k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d2k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FARP2_MOUSE FARP2_MOUSE]] Rho-guanine nucleotide exchange factor that activates RAC1. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton.<ref>PMID:12351724</ref> <ref>PMID:16286926</ref> | + | [https://www.uniprot.org/uniprot/FARP2_MOUSE FARP2_MOUSE] Rho-guanine nucleotide exchange factor that activates RAC1. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton.<ref>PMID:12351724</ref> <ref>PMID:16286926</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: He, X]] | + | [[Category: He X]] |
| - | [[Category: Zhang, X]] | + | [[Category: Zhang X]] |
| - | [[Category: Membrane targeting]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
FARP2_MOUSE Rho-guanine nucleotide exchange factor that activates RAC1. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton.[1] [2]
Publication Abstract from PubMed
FARP1 is a multi-domain protein that is involved in regulating neuronal development through interacting with cell surface proteins such as class A Plexins and SynCAM 1. The N-terminal FERM domain in FARP1 is known to both promote membrane localization and mediate these protein interactions, for which the underlying molecular mechanisms remain unclear. Here we determined the crystal structures of the FERM domain of FARP1 from zebrafish, and those of FARP2 (a close homolog of FARP1) from mouse and zebrafish. These FERM domains adopt the three-leaved clover fold that is typical of all FERM domains. Our structures reveal a positively charged surface patch that is highly conserved in the FERM domain of FARP1 and FARP2. In vitro lipid-binding experiments showed that the FARP1 FERM domain binds specifically to several types of phospholipid, which is dependent on the positively charged surface patch. We further determined through cell-based analyses that this surface patch on the FERM domain underlies the localization of FARP1 to the plasma membrane, and that FERM domain interactions recruit it to postsynaptic sites in neurons.
Structural analyses of FERM domain-mediated membrane localization of FARP1.,Kuo YC, He X, Coleman AJ, Chen YJ, Dasari P, Liou J, Biederer T, Zhang X Sci Rep. 2018 Jul 11;8(1):10477. doi: 10.1038/s41598-018-28692-4. PMID:29992992[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kubo T, Yamashita T, Yamaguchi A, Sumimoto H, Hosokawa K, Tohyama M. A novel FERM domain including guanine nucleotide exchange factor is involved in Rac signaling and regulates neurite remodeling. J Neurosci. 2002 Oct 1;22(19):8504-13. PMID:12351724
- ↑ Toyofuku T, Yoshida J, Sugimoto T, Zhang H, Kumanogoh A, Hori M, Kikutani H. FARP2 triggers signals for Sema3A-mediated axonal repulsion. Nat Neurosci. 2005 Dec;8(12):1712-9. Epub 2005 Nov 13. PMID:16286926 doi:nn1596
- ↑ Kuo YC, He X, Coleman AJ, Chen YJ, Dasari P, Liou J, Biederer T, Zhang X. Structural analyses of FERM domain-mediated membrane localization of FARP1. Sci Rep. 2018 Jul 11;8(1):10477. doi: 10.1038/s41598-018-28692-4. PMID:29992992 doi:http://dx.doi.org/10.1038/s41598-018-28692-4
|
