3hr0: Difference between revisions

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 <StructureSection load='3hr0' size='340' side='right'caption='[[3hr0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3hr0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HR0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3hr0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HR0 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COG4, COG4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=3hr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hr0 OCA], [https://pdbe.org/3hr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hr0 RCSB], [https://www.ebi.ac.uk/pdbsum/3hr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hr0 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/COG4_HUMAN COG4_HUMAN]] Defects in COG4 are the cause of congenital disorder of glycosylation type 2J (CDG2J) [MIM:[https://omim.org/entry/613489 613489]]. It is a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.<ref>PMID:19651599</ref> <ref>PMID:19494034</ref>
+[https://www.uniprot.org/uniprot/COG4_HUMAN COG4_HUMAN] Defects in COG4 are the cause of congenital disorder of glycosylation type 2J (CDG2J) [MIM:[https://omim.org/entry/613489 613489]. It is a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.<ref>PMID:19651599</ref> <ref>PMID:19494034</ref>
 == Function ==
-[[https://www.uniprot.org/uniprot/COG4_HUMAN COG4_HUMAN]] Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1.<ref>PMID:19536132</ref>
+[https://www.uniprot.org/uniprot/COG4_HUMAN COG4_HUMAN] Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1.<ref>PMID:19536132</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hr0 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The proper glycosylation of proteins trafficking through the Golgi apparatus depends upon the conserved oligomeric Golgi (COG) complex. Defects in COG can cause fatal congenital disorders of glycosylation (CDGs) in humans. The recent discovery of a form of CDG, caused in part by a COG4 missense mutation changing Arg 729 to Trp, prompted us to determine the 1.9 A crystal structure of a Cog4 C-terminal fragment. Arg 729 is found to occupy a key position at the center of a salt bridge network, thereby stabilizing Cog4's small C-terminal domain. Studies in HeLa cells reveal that this C-terminal domain, while not needed for the incorporation of Cog4 into COG complexes, is essential for the proper glycosylation of cell surface proteins. We also find that Cog4 bears a strong structural resemblance to exocyst and Dsl1p complex subunits. These complexes and others have been proposed to function by mediating the initial tethering between transport vesicles and their membrane targets; the emerging structural similarities provide strong evidence of a common evolutionary origin and may reflect shared mechanisms of action.
-Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene.,Richardson BC, Smith RD, Ungar D, Nakamura A, Jeffrey PD, Lupashin VV, Hughson FM Proc Natl Acad Sci U S A. 2009 Jul 27. PMID:19651599<ref>PMID:19651599</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3hr0" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Hughson, F M]]
+[[Category: Hughson FM]]
-[[Category: Jeffrey, P D]]
+[[Category: Jeffrey PD]]
-[[Category: Nakamura, A]]
+[[Category: Nakamura A]]
-[[Category: Richardson, B C]]
+[[Category: Richardson BC]]
-[[Category: Ungar, D]]
+[[Category: Ungar D]]
-[[Category: Alternative splicing]]
-[[Category: Conserved oligomeric golgi complex]]
-[[Category: Exocyst]]
-[[Category: Golgi apparatus]]
-[[Category: Intracellular trafficking]]
-[[Category: Membrane]]
-[[Category: Multisubunit tethering complex]]
-[[Category: Phosphoprotein]]
-[[Category: Protein transport]]
-[[Category: Transport]]
-[[Category: Transport protein]]
-[[Category: Vesicle tethering]]