2lat
From Proteopedia
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| - | {{STRUCTURE_2lat| PDB=2lat | SCENE= }} | ||
| - | ===Solution structure of a Human minimembrane protein OST4=== | ||
| - | {{ABSTRACT_PUBMED_21609714}} | ||
| - | == | + | ==Solution structure of a Human minimembrane protein OST4== |
| - | [[2lat]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAT OCA]. | + | <StructureSection load='2lat' size='340' side='right'caption='[[2lat]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lat]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LAT FirstGlance]. <br> | ||
| + | </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=2lat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lat OCA], [https://pdbe.org/2lat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lat RCSB], [https://www.ebi.ac.uk/pdbsum/2lat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lat ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OST4_HUMAN OST4_HUMAN] May be involved in N-glycosylation through its association with N-oligosaccharyl transferase (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Oligosaccharyltransferase (OST) is a membrane associated enzyme complex that mediates transfer of an oligosaccharide onto asparagine residue of a protein. Human Ost4 is a small membrane protein and belongs to one of the seven subunits of human OST. This study determined the solution structure of human Ost4 in solvent system using NMR spectroscopy. Ost4 was demonstrated that the residues 5-30 adopt an alpha-helical structure. A kink structure was observed in the transmembrane domain, which may be important for its function. | ||
| - | + | Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex.,Gayen S, Kang C Biochem Biophys Res Commun. 2011 Jun 10;409(3):572-6. Epub 2011 May 15. PMID:21609714<ref>PMID:21609714</ref> | |
| - | <ref | + | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2lat" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gayen S]] | ||
| + | [[Category: Kang C]] | ||
Current revision
Solution structure of a Human minimembrane protein OST4
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