3mv2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
{{Seed}}
[[Image:3mv2.png|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_3mv2", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_3mv2|  PDB=3mv2  |  SCENE=  }}  
{{STRUCTURE_3mv2|  PDB=3mv2  |  SCENE=  }}  
===Crystal Structure of a-COP in Complex with e-COP===
===Crystal Structure of a-COP in Complex with e-COP===
{{ABSTRACT_PUBMED_20534429}}


 
==Function==
<!--  
[[http://www.uniprot.org/uniprot/COPA_YEAST COPA_YEAST]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.<ref>PMID:17101773</ref>  [[http://www.uniprot.org/uniprot/COPE_YEAST COPE_YEAST]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).<ref>PMID:9463377</ref> <ref>PMID:17101773</ref> 
The line below this paragraph, {{ABSTRACT_PUBMED_20534429}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 20534429 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_20534429}}


==About this Structure==
==About this Structure==
3MV2 is a 6 chains structure with sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MV2 OCA].  
[[3mv2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MV2 OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:20534429</ref><references group="xtra"/>
<ref group="xtra">PMID:020534429</ref><references group="xtra"/><references/>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Hoelz, A.]]
[[Category: Hoelz, A.]]
Line 29: Line 16:
[[Category: Protein transport]]
[[Category: Protein transport]]
[[Category: Vesicular membrane coat coat protein complex i]]
[[Category: Vesicular membrane coat coat protein complex i]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  7 07:55:35 2010''