4gmv: Difference between revisions

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~~{{STRUCTURE_4gmv| PDB=4gmv | SCENE= }}~~

==Crystal Structure of the coiled-coil, RA and PH domains of Lamellipodin==

===Crystal Structure of the coiled-coil, RA and PH domains of Lamellipodin===

~~{{ABSTRACT_PUBMED_23483482}}~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4gmv]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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>

<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 Homo sapiens])</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=4gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gmv RCSB], [http://www.ebi.ac.uk/pdbsum/4gmv PDBsum]</span></td></tr>

</table>

== 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.

~~==Function==~~

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<ref>PMID:23483482</ref>

~~[[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~~.

==~~About this Structure~~==

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

~~[[4gmv]] is a 2 chain structure with sequence from [http:~~//~~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].~~

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Chang, Y C.E.]]

[[Category: Chang, Y C.E]]

[[Category: Wu, J.]]

[[Category: Wu, J]]

[[Category: Cell adhesion]]

[[Category: Cell migration]]

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_4gmv|  PDB=4gmv  |  SCENE=  }}
+==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]] 2.40&Aring;' scene=''>
-{{ABSTRACT_PUBMED_23483482}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4gmv]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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>
+<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 Homo sapiens])</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=4gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gmv RCSB], [http://www.ebi.ac.uk/pdbsum/4gmv PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== 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.
-==Function==
+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<ref>PMID:23483482</ref>
-[[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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[4gmv]] is a 2 chain structure with sequence from [http://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].
+</div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Chang, Y C.E.]]
+[[Category: Chang, Y C.E]]
-[[Category: Wu, J.]]
+[[Category: Wu, J]]
 [[Category: Cell adhesion]]
 [[Category: Cell migration]]