1p23

From Proteopedia

(Difference between revisions)

Revision as of 07:55, 11 September 2015

STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION, NMR, 10 STRUCTURES

Structural highlights

1p23 is a 4 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TMEDA_RABIT] Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act togther with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus (By similarity).^[1]

Publication Abstract from PubMed

Coatomer, the coat protein complex of coat protein (COPI) vesicles, is involved in the budding of these vesicles. Its interaction with the cytoplasmic domains of some p24-family members, type I transmembrane proteins of the Golgi, has been shown to induce a conformational change of coatomer that initiates polymerization of the complex. From stoichiometrical data it is likely that interaction of coatomer with the small tail domains involves an oligomeric form of the p24 proteins. Here we present the structure of peptide analogs of the cytoplasmic domain of p23, a member of the p24 family, as determined by two-dimensional nuclear magnetic resonance spectroscopy in the presence of 2,2,2-trifluoroethanol. An improved strategy for structure calculation revealed that the tail domain peptides form alpha-helices and adopt a tetrameric state. Based on these results we propose an initial model for the binding of coatomer by p23 and the induced conformational change of coatomer that results in its polymerization, curvature of the Golgi membrane to form a bud, and finally a COPI-coated vesicle.

Structure of the cytoplasmic domain of p23 in solution: implications for the formation of COPI vesicles.,Weidler M, Reinhard C, Friedrich G, Wieland FT, Rosch P Biochem Biophys Res Commun. 2000 May 10;271(2):401-8. PMID:10799309^[2]

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

References

↑ Majoul I, Sohn K, Wieland FT, Pepperkok R, Pizza M, Hillemann J, Soling HD. KDEL receptor (Erd2p)-mediated retrograde transport of the cholera toxin A subunit from the Golgi involves COPI, p23, and the COOH terminus of Erd2p. J Cell Biol. 1998 Nov 2;143(3):601-12. PMID:9813083
↑ Weidler M, Reinhard C, Friedrich G, Wieland FT, Rosch P. Structure of the cytoplasmic domain of p23 in solution: implications for the formation of COPI vesicles. Biochem Biophys Res Commun. 2000 May 10;271(2):401-8. PMID:10799309 doi:10.1006/bbrc.2000.2511

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/1p23"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1p23]] is a 4 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P23 FirstGlance]. <br>
-</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=1p23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p23 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p23 RCSB], [http://www.ebi.ac.uk/pdbsum/1p23 PDBsum]</span></td></tr>
+</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=1p23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p23 OCA], [http://pdbe.org/1p23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p23 RCSB], [http://www.ebi.ac.uk/pdbsum/1p23 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 15: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1p23" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1p23

From Proteopedia

Revision as of 07:55, 11 September 2015

STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION, NMR, 10 STRUCTURES

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox