1eq1: Difference between revisions
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|RELATEDENTRY=[[1aep|1AEP]], [[1lpe|1LPE]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq1 OCA], [http://www.ebi.ac.uk/pdbsum/1eq1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eq1 RCSB]</span> | |||
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[[Category: five helix-bundle]] | [[Category: five helix-bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:31 2008'' | ||
Revision as of 20:07, 30 March 2008
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| Related: | 1AEP, 1LPE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III
OverviewOverview
The high-resolution NMR structure of apolipophorin III from the sphinx moth, Manduca sexta, has been determined in the lipid-free state. We show that lipid-free apolipophorin III adopts a unique helix-bundle topology that has several characteristic structural features. These include a marginally stable, up-and-down helix bundle that allows for concerted opening of the bundle about "hinged" loops upon lipid interaction and buried polar/ionizable residues and buried interhelical H-bonds located in the otherwise hydrophobic interior of the bundle that adjust protein stability and facilitate lipid-induced conformational opening. We suggest that these structural features modulate the conformational adaptability of the lipid-free helix bundle upon lipid binding and control return of the open conformation to the original lipid-free helix-bundle state. Taken together, these data provide a structural rationale for the ability of exchangeable apolipoproteins to reversibly interact with circulating lipoprotein particles.
About this StructureAbout this Structure
1EQ1 is a Single protein structure of sequence from Manduca sexta. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein., Wang J, Sykes BD, Ryan RO, Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1188-93. Epub 2002 Jan 29. PMID:11818551
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