1gv9

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(New page: 200px<br /><applet load="1gv9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gv9, resolution 1.46&Aring;" /> '''P58/ERGIC-53'''<br /...)
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[[Image:1gv9.jpg|left|200px]]<br /><applet load="1gv9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gv9, resolution 1.46&Aring;" />
 
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'''P58/ERGIC-53'''<br />
 
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==Overview==
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==p58/ERGIC-53==
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p58/ERGIC-53 is an animal calcium-dependent lectin that cycles between the, endoplasmic reticulum (ER) and the Golgi complex and appears to act as a, cargo receptor for a subset of soluble glycoproteins exported from the ER., We have determined the crystal structure of the carbohydrate recognition, domain (CRD) of p58, the rat homologue of human ERGIC-53, to 1.46 A, resolution. The fold and ligand binding site are most similar to those of, leguminous lectins. The structure also resembles that of the CRD of the ER, folding chaperone calnexin and the neurexins, a family of non-lectin, proteins expressed on neurons. The CRD comprises one concave and one, convex beta-sheet packed into a beta-sandwich. The ligand binding site, resides in a negatively charged cleft formed by conserved residues. A, large surface patch of conserved residues with a putative role in, protein-protein interactions and oligomerization lies on the opposite side, of the ligand binding site. Together with previous functional data, the, structure defines a new and expanding class of calcium-dependent animal, lectins and provides a starting point for the understanding of, glycoprotein sorting between the ER and the Golgi.
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<StructureSection load='1gv9' size='340' side='right'caption='[[1gv9]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GV9 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">X-ray diffraction, [[Resolution|Resolution]] 1.46&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1gv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gv9 OCA], [https://pdbe.org/1gv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gv9 RCSB], [https://www.ebi.ac.uk/pdbsum/1gv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gv9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LMAN1_RAT LMAN1_RAT] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gv/1gv9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1gv9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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p58/ERGIC-53 is an animal calcium-dependent lectin that cycles between the endoplasmic reticulum (ER) and the Golgi complex and appears to act as a cargo receptor for a subset of soluble glycoproteins exported from the ER. We have determined the crystal structure of the carbohydrate recognition domain (CRD) of p58, the rat homologue of human ERGIC-53, to 1.46 A resolution. The fold and ligand binding site are most similar to those of leguminous lectins. The structure also resembles that of the CRD of the ER folding chaperone calnexin and the neurexins, a family of non-lectin proteins expressed on neurons. The CRD comprises one concave and one convex beta-sheet packed into a beta-sandwich. The ligand binding site resides in a negatively charged cleft formed by conserved residues. A large surface patch of conserved residues with a putative role in protein-protein interactions and oligomerization lies on the opposite side of the ligand binding site. Together with previous functional data, the structure defines a new and expanding class of calcium-dependent animal lectins and provides a starting point for the understanding of glycoprotein sorting between the ER and the Golgi.
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==About this Structure==
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Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum.,Velloso LM, Svensson K, Schneider G, Pettersson RF, Lindqvist Y J Biol Chem. 2002 May 3;277(18):15979-84. Epub 2002 Feb 15. PMID:11850423<ref>PMID:11850423</ref>
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1GV9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GV9 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum., Velloso LM, Svensson K, Schneider G, Pettersson RF, Lindqvist Y, J Biol Chem. 2002 May 3;277(18):15979-84. Epub 2002 Feb 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11850423 11850423]
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</div>
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[[Category: Rattus norvegicus]]
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<div class="pdbe-citations 1gv9" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Lindqvist, Y.]]
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[[Category: Pettersson, R.F.]]
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[[Category: Schneider, G.]]
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[[Category: Svensson, K.]]
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[[Category: Velloso, L.M.]]
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[[Category: SO4]]
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[[Category: carbohydrate binding]]
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[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:18:22 2007''
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==See Also==
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*[[ERGIC-53|ERGIC-53]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
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[[Category: Lindqvist Y]]
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[[Category: Pettersson RF]]
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[[Category: Schneider G]]
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[[Category: Svensson K]]
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[[Category: Velloso LM]]

Current revision

p58/ERGIC-53

PDB ID 1gv9

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