This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2j1d

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:58, 19 January 2022

Crystallization of hDaam1 C-terminal Fragment

Structural highlights

2j1d is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DAAM1_HUMAN] Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments.^[1] ^[2]

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

Daam1 (dishevelled-associated activator of morphogenesis-1) is a diaphanous-related formin first studied as a novel dishevelled binding protein and shown to be crucial for the planar cell polarity (PCP) pathway in Xenopus. Daam1, like other formins, directs nucleation and elongation of new actin filaments using its conserved formin-homology-2 (FH2) domain. Here we report the crystal structure of a large C-terminal fragment of human Daam1 containing the FH2 domain. The structure, determined at 2.25 A resolution using the single-wavelength anomalous diffraction (SAD) phasing method, reveals a "tethered dimer" architecture that is similar to that previously described for the FH2 domain of the yeast formin Bni1, which shares approximately 21% sequence identity with Daam1. Despite the overall similarity with the dimeric FH2 domain of Bni1 and with a truncated monomeric structure of mDia1, the Daam1 FH2 structure reveals a number of differences in secondary structure elements and in the "lasso/post" dimerization interface that may be functionally important. Most strikingly, the two halves of the crystallographic dimer pack together in a manner that occludes their actin binding surfaces. This "locked" conformation is stabilized by two novel, interacting beta-strands formed by the ends of the linkers that connect the two sides of the dimer. The Daam1 FH2 domain has weak actin assembly activity as compared with other mammalian formins, but mutations that disrupt the beta-strand lock increase activity about tenfold to a level comparable to other formins, suggesting that this occluded conformation may represent an auto-inhibited conformation of the Daam1 FH2 domain.

Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly.,Lu J, Meng W, Poy F, Maiti S, Goode BL, Eck MJ J Mol Biol. 2007 Jun 22;369(5):1258-69. Epub 2007 Apr 5. PMID:17482208^[3]

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

References

↑ Aspenstrom P, Richnau N, Johansson AS. The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics. Exp Cell Res. 2006 Jul 15;312(12):2180-94. Epub 2006 Apr 21. PMID:16630611 doi:http://dx.doi.org/10.1016/j.yexcr.2006.03.013
↑ Lu J, Meng W, Poy F, Maiti S, Goode BL, Eck MJ. Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly. J Mol Biol. 2007 Jun 22;369(5):1258-69. Epub 2007 Apr 5. PMID:17482208 doi:10.1016/j.jmb.2007.04.002
↑ Lu J, Meng W, Poy F, Maiti S, Goode BL, Eck MJ. Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly. J Mol Biol. 2007 Jun 22;369(5):1258-69. Epub 2007 Apr 5. PMID:17482208 doi:10.1016/j.jmb.2007.04.002

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j1d"

@@ Line 3: / Line 3: @@
 <StructureSection load='2j1d' size='340' side='right'caption='[[2j1d]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2j1d]] is a 1 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=2J1D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2J1D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2j1d]] 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=2J1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J1D FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2j1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1d OCA], [http://pdbe.org/2j1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j1d RCSB], [http://www.ebi.ac.uk/pdbsum/2j1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j1d 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=2j1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1d OCA], [https://pdbe.org/2j1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j1d RCSB], [https://www.ebi.ac.uk/pdbsum/2j1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j1d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DAAM1_HUMAN DAAM1_HUMAN]] Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments.<ref>PMID:16630611</ref> <ref>PMID:17482208</ref>
+[[https://www.uniprot.org/uniprot/DAAM1_HUMAN DAAM1_HUMAN]] Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments.<ref>PMID:16630611</ref> <ref>PMID:17482208</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2j1d

From Proteopedia

Revision as of 07:58, 19 January 2022

Crystallization of hDaam1 C-terminal Fragment

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox