1eq1: Difference between revisions

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[[Image:1eq1.gif|left|200px]]
[[Image:1eq1.gif|left|200px]]


{{Structure
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{{STRUCTURE_1eq1|  PDB=1eq1 |  SCENE= }}  
|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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'''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III'''
'''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III'''
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[[Category: Sykes, B D.]]
[[Category: Sykes, B D.]]
[[Category: Wang, J.]]
[[Category: Wang, J.]]
[[Category: helix-short helix-helix recognition motif]]
[[Category: Helix-short helix-helix recognition motif]]
[[Category: five helix-bundle]]
[[Category: Five helix-bundle]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:23:35 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:31 2008''

Revision as of 15:23, 2 May 2008

File:1eq1.gif

Template:STRUCTURE 1eq1

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 Page seeded by OCA on Fri May 2 15:23:35 2008

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