3zee

From Proteopedia

(Difference between revisions)

Revision as of 23:56, 24 December 2014

Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain

Structural highlights

3zee is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PARD3_RAT] Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (By similarity). Targets the phosphatase PTEN to cell junctions.^[1] ^[2]

Publication Abstract from PubMed

Par-3, the central organizer of the Par-3/Par-6/atypical protein kinase C complex, is a multimodular scaffold protein that is essential for cell polarity establishment and maintenance. The N-terminal domain (NTD) of Par-3 is capable of self-association to form filament-like structures, although the underlying mechanism is poorly understood. Here, we determined the crystal structure of Par-3 NTD and solved the filament structure by cryoelectron microscopy. We found that an intrinsic "front-to-back" interaction mode is important for Par-3 NTD self-association and that both the lateral and longitudinal packing within the filament are mediated by electrostatic interactions. Disruptions of the lateral or longitudinal packing significantly impaired Par-3 NTD self-association and thereby impacted the Par-3-mediated epithelial polarization. We finally demonstrated that a Par-3 NTD-like domain from histidine ammonia-lyase also harbors a similar self-association capacity. This work unequivocally provides the structural basis for Par-3 NTD self-association and characterizes one type of protein domain that can self-assemble via electrostatic interactions.

Structural insights into the intrinsic self-assembly of par-3 N-terminal domain.,Zhang Y, Wang W, Chen J, Zhang K, Gao F, Gao B, Zhang S, Dong M, Besenbacher F, Gong W, Zhang M, Sun F, Feng W Structure. 2013 Jun 4;21(6):997-1006. doi: 10.1016/j.str.2013.04.004. Epub 2013, May 2. PMID:23643951^[3]

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

References

↑ Wu H, Feng W, Chen J, Chan LN, Huang S, Zhang M. PDZ domains of Par-3 as potential phosphoinositide signaling integrators. Mol Cell. 2007 Dec 14;28(5):886-98. PMID:18082612 doi:10.1016/j.molcel.2007.10.028
↑ Feng W, Wu H, Chan LN, Zhang M. Par-3-mediated junctional localization of the lipid phosphatase PTEN is required for cell polarity establishment. J Biol Chem. 2008 Aug 22;283(34):23440-9. doi: 10.1074/jbc.M802482200. Epub 2008 , Jun 10. PMID:18550519 doi:10.1074/jbc.M802482200
↑ Zhang Y, Wang W, Chen J, Zhang K, Gao F, Gao B, Zhang S, Dong M, Besenbacher F, Gong W, Zhang M, Sun F, Feng W. Structural insights into the intrinsic self-assembly of par-3 N-terminal domain. Structure. 2013 Jun 4;21(6):997-1006. doi: 10.1016/j.str.2013.04.004. Epub 2013, May 2. PMID:23643951 doi:10.1016/j.str.2013.04.004

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/3zee"

@@ Line 5: / Line 5: @@
 </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=3zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zee RCSB], [http://www.ebi.ac.uk/pdbsum/3zee PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PARD3_RAT PARD3_RAT]] Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (By similarity). Targets the phosphatase PTEN to cell junctions.<ref>PMID:18082612</ref> <ref>PMID:18550519</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3zee

From Proteopedia

Revision as of 23:56, 24 December 2014

Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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