We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1m23

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (18:49, 29 November 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1m23.png|left|200px]]
 
-
<!--
+
==STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION==
-
The line below this paragraph, containing "STRUCTURE_1m23", creates the "Structure Box" on the page.
+
<StructureSection load='1m23' size='340' side='right'caption='[[1m23]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1m23]] is a 1 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=1M23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M23 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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=1m23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m23 OCA], [https://pdbe.org/1m23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m23 RCSB], [https://www.ebi.ac.uk/pdbsum/1m23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m23 ProSAT]</span></td></tr>
-
{{STRUCTURE_1m23| PDB=1m23 | SCENE= }}
+
</table>
 +
== Function ==
 +
[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>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Coatomer, the coat protein complex of COPI vesicles, is involved in the budding of these vesicles, but the underlying mechanism is unknown. Toward a better understanding of this process, the interaction between coatomer and the cytoplasmic domain of a major transmembrane protein of COPI vesicles, p23, was studied. Interaction of coatomer with this peptide domain results in a conformational change and polymerization of the complex in vitro. This changed conformation also is observed in vivo, i.e., on the surface of authentic, isolated COPI vesicles. An average of four peptides was found associated with one coatomer complex after polymerization. Based on these results, we propose a mechanism by which the induced conformational change of coatomer results in its polymerization, and thus drives formation of the bud on the Golgi membrane during biogenesis of a COPI vesicle.
-
===STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION===
+
Receptor-induced polymerization of coatomer.,Reinhard C, Harter C, Bremser M, Brugger B, Sohn K, Helms JB, Wieland F Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1224-8. PMID:9990005<ref>PMID:9990005</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_9990005}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1m23" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 9990005 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_9990005}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
1M23 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M23 OCA].
+
[[Category: Oryctolagus cuniculus]]
-
 
+
[[Category: Reinhard C]]
-
==Reference==
+
[[Category: Roesch P]]
-
Receptor-induced polymerization of coatomer., Reinhard C, Harter C, Bremser M, Brugger B, Sohn K, Helms JB, Wieland F, Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1224-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9990005 9990005]
+
[[Category: Weidler M]]
-
[[Category: Single protein]]
+
[[Category: Wieland F]]
-
[[Category: Reinhard, C.]]
+
-
[[Category: Roesch, P.]]
+
-
[[Category: Weidler, M.]]
+
-
[[Category: Wieland, F.]]
+
-
[[Category: Coatomer]]
+
-
[[Category: Cop]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Golgi stack]]
+
-
[[Category: P23 family]]
+
-
[[Category: Protein transport]]
+
-
[[Category: Signal]]
+
-
[[Category: Solution structure]]
+
-
[[Category: Transmembrane]]
+
-
[[Category: Transport]]
+
-
[[Category: Vesicular transport]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:03:15 2008''
+

Current revision

STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION

PDB ID 1m23

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m23"
Personal tools