2lhk
From Proteopedia
(Difference between revisions)
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<StructureSection load='2lhk' size='340' side='right' caption='[[2lhk]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='2lhk' size='340' side='right' caption='[[2lhk]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2lhk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHK OCA]. | + | <table><tr><td colspan='2'>[[2lhk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LHK FirstGlance]. <br> |
- | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lhk RCSB], [http://www.ebi.ac.uk/pdbsum/2lhk PDBsum]</span></td></tr> | |
- | <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=2lhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lhk RCSB], [http://www.ebi.ac.uk/pdbsum/2lhk PDBsum]</span></td></tr> | + | </table> |
- | <table> | + | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Structural instability tuning as a regulatory mechanism in protein-protein interactions.,Chen L, Balabanidou V, Remeta DP, Minetti CA, Portaliou AG, Economou A, Kalodimos CG Mol Cell. 2011 Dec 9;44(5):734-44. PMID:22152477<ref>PMID:22152477</ref> | Structural instability tuning as a regulatory mechanism in protein-protein interactions.,Chen L, Balabanidou V, Remeta DP, Minetti CA, Portaliou AG, Economou A, Kalodimos CG Mol Cell. 2011 Dec 9;44(5):734-44. PMID:22152477<ref>PMID:22152477</ref> | ||
- | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: Chen, L | + | [[Category: Chen, L]] |
- | [[Category: Economou, A | + | [[Category: Economou, A]] |
- | [[Category: Kalodimos, C G | + | [[Category: Kalodimos, C G]] |
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Helical bundle]] | [[Category: Helical bundle]] | ||
[[Category: Type iii secretion system]] | [[Category: Type iii secretion system]] |
Revision as of 06:52, 22 December 2014
Structural analysis of a chaperone in type III secretion system
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