1jhn

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[[Image:1jhn.png|left|200px]]
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==Crystal Structure of the Lumenal Domain of Calnexin==
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<StructureSection load='1jhn' size='340' side='right' caption='[[1jhn]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JHN FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jhn RCSB], [http://www.ebi.ac.uk/pdbsum/1jhn PDBsum]</span></td></tr>
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<table>
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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/jh/1jhn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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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The three-dimensional structure of the lumenal domain of the lectin-like chaperone calnexin determined to 2.9 A resolution reveals an extended 140 A arm inserted into a beta sandwich structure characteristic of legume lectins. The arm is composed of tandem repeats of two proline-rich sequence motifs which interact with one another in a head-to-tail fashion. Identification of the ligand binding site establishes calnexin as a monovalent lectin, providing insight into the mechanism by which the calnexin family of chaperones interacts with monoglucosylated glycoproteins.
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{{STRUCTURE_1jhn| PDB=1jhn | SCENE= }}
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The Structure of calnexin, an ER chaperone involved in quality control of protein folding.,Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M Mol Cell. 2001 Sep;8(3):633-44. PMID:11583625<ref>PMID:11583625</ref>
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===Crystal Structure of the Lumenal Domain of Calnexin===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_11583625}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1jhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHN OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:011583625</ref><references group="xtra"/>
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[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
[[Category: Bergeron, J M.]]
[[Category: Bergeron, J M.]]

Revision as of 09:30, 28 September 2014

Crystal Structure of the Lumenal Domain of Calnexin

1jhn, resolution 2.90Å

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