1p23

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[[Image:1p23.png|left|200px]]
 
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==STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION, NMR, 10 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1p23", creates the "Structure Box" on the page.
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<StructureSection load='1p23' size='340' side='right'caption='[[1p23]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1p23]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1P23 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p23 OCA], [https://pdbe.org/1p23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p23 RCSB], [https://www.ebi.ac.uk/pdbsum/1p23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p23 ProSAT]</span></td></tr>
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{{STRUCTURE_1p23| PDB=1p23 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TMEDA_RABIT 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).<ref>PMID:9813083</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION, NMR, 10 STRUCTURES===
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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<ref>PMID:10799309</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1p23" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10799309 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10799309}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1P23 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P23 OCA].
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[[Category: Oryctolagus cuniculus]]
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[[Category: Reinhard C]]
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==Reference==
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[[Category: Roesch P]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10799309 10799309]
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[[Category: Weidler M]]
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[[Category: Single protein]]
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[[Category: Wieland FT]]
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[[Category: Reinhard, C.]]
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[[Category: Roesch, P.]]
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[[Category: Weidler, M.]]
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[[Category: Wieland, F T.]]
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[[Category: Coatomer]]
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[[Category: Cop]]
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[[Category: Glycoprotein]]
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[[Category: Golgi stack]]
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[[Category: Integral membrane protein]]
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[[Category: P24 family]]
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[[Category: Protein transport]]
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[[Category: Signal]]
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[[Category: Solution structure]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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[[Category: Vesicular transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:27:31 2008''
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Current revision

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

PDB ID 1p23

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