2lqr
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lqr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQR FirstGlance]. <br> | <table><tr><td colspan='2'>[[2lqr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQR FirstGlance]. <br> | ||
| - | </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=2lqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqr OCA], [https://pdbe.org/2lqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqr RCSB], [https://www.ebi.ac.uk/pdbsum/2lqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqr ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqr OCA], [https://pdbe.org/2lqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqr RCSB], [https://www.ebi.ac.uk/pdbsum/2lqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PALLD_MOUSE PALLD_MOUSE] Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific May be required for the initiation of neural tube closure.<ref>PMID:10931874</ref> <ref>PMID:15950489</ref> <ref>PMID:16492705</ref> <ref>PMID:17115415</ref> | [https://www.uniprot.org/uniprot/PALLD_MOUSE PALLD_MOUSE] Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific May be required for the initiation of neural tube closure.<ref>PMID:10931874</ref> <ref>PMID:15950489</ref> <ref>PMID:16492705</ref> <ref>PMID:17115415</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Here, we report the NMR structure of the actin-binding domain contained in the cell adhesion protein palladin. Previously, we demonstrated that one of the immunoglobulin domains of palladin (Ig3) is both necessary and sufficient for direct filamentous actin binding in vitro. In this study, we identify two basic patches on opposite faces of Ig3 that are critical for actin binding and cross-linking. Sedimentation equilibrium assays indicate that the Ig3 domain of palladin does not self-associate. These combined data are consistent with an actin cross-linking mechanism that involves concurrent attachment of two actin filaments by a single palladin molecule by an electrostatic mechanism. Palladin mutations that disrupt actin binding show altered cellular distributions and morphology of actin in cells, revealing a functional requirement for the interaction between palladin and actin in vivo. | ||
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| - | Structure and Function of Palladin's Actin Binding Domain.,Beck MR, Dixon RD, Goicoechea SM, Murphy GS, Brungardt JG, Beam MT, Srinath P, Patel J, Mohiuddin J, Otey CA, Campbell SL J Mol Biol. 2013 Jun 25. pii: S0022-2836(13)00395-1. doi:, 10.1016/j.jmb.2013.06.016. PMID:23806659<ref>PMID:23806659</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2lqr" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
NMR structure of Ig3 domain of palladin
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