2lqr

From Proteopedia

(Difference between revisions)

Revision as of 17:54, 25 December 2014

NMR structure of Ig3 domain of palladin

Structural highlights

2lqr is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Palld, Kiaa0992 (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] ^[4]

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.

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^[5]

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

References

↑ Parast MM, Otey CA. Characterization of palladin, a novel protein localized to stress fibers and cell adhesions. J Cell Biol. 2000 Aug 7;150(3):643-56. PMID:10931874
↑ Luo H, Liu X, Wang F, Huang Q, Shen S, Wang L, Xu G, Sun X, Kong H, Gu M, Chen S, Chen Z, Wang Z. Disruption of palladin results in neural tube closure defects in mice. Mol Cell Neurosci. 2005 Aug;29(4):507-15. PMID:15950489 doi:10.1016/j.mcn.2004.12.002
↑ Rachlin AS, Otey CA. Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin. J Cell Sci. 2006 Mar 15;119(Pt 6):995-1004. Epub 2006 Feb 21. PMID:16492705 doi:10.1242/jcs.02825
↑ Liu XS, Luo HJ, Yang H, Wang L, Kong H, Jin YE, Wang F, Gu MM, Chen Z, Lu ZY, Wang ZG. Palladin regulates cell and extracellular matrix interaction through maintaining normal actin cytoskeleton architecture and stabilizing beta1-integrin. J Cell Biochem. 2007 Apr 1;100(5):1288-300. PMID:17115415 doi:10.1002/jcb.21126
↑ Beck MR, Dixon RD, Goicoechea SM, Murphy GS, Brungardt JG, Beam MT, Srinath P, Patel J, Mohiuddin J, Otey CA, Campbell SL. Structure and Function of Palladin's Actin Binding Domain. J Mol Biol. 2013 Jun 25. pii: S0022-2836(13)00395-1. doi:, 10.1016/j.jmb.2013.06.016. PMID:23806659 doi:10.1016/j.jmb.2013.06.016

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 6: / Line 6: @@
 <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=2lqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lqr RCSB], [http://www.ebi.ac.uk/pdbsum/2lqr PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==

2lqr

From Proteopedia

Revision as of 17:54, 25 December 2014

NMR structure of Ig3 domain of palladin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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