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| - | {{STRUCTURE_2lqr| PDB=2lqr | SCENE= }} | |
| - | ===NMR structure of Ig3 domain of palladin=== | |
| - | {{ABSTRACT_PUBMED_23806659}} | |
| | | | |
| - | ==Function== | + | ==NMR structure of Ig3 domain of palladin== |
| - | [[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> | + | <StructureSection load='2lqr' size='340' side='right'caption='[[2lqr]]' scene=''> |
| - | | + | == Structural highlights == |
| - | ==About this Structure== | + | <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> |
| - | [[2lqr]] is a 1 chain structure with sequence from [http://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].
| + | </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> |
| - | ==Reference==
| + | </table> |
| - | <ref group="xtra">PMID:023806659</ref><references group="xtra"/><references/>
| + | == 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> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Beck, M R.]] | + | [[Category: Beck MR]] |
| - | [[Category: Campbell, S L.]] | + | [[Category: Campbell SL]] |
| - | [[Category: IV, R D.S Dixon.]] | + | [[Category: Dixon IV RDS]] |
| - | [[Category: Murphy, G S.]] | + | [[Category: Murphy GS]] |
| - | [[Category: Otey, C A.]] | + | [[Category: Otey CA]] |
| - | [[Category: Actin binding protein]]
| + | |
| - | [[Category: Immunoglubulin]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
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]
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
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