1eq1: Difference between revisions
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[[Image:1eq1.gif|left|200px]] | [[Image:1eq1.gif|left|200px]] | ||
'''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III''' | {{Structure | ||
|PDB= 1eq1 |SIZE=350|CAPTION= <scene name='initialview01'>1eq1</scene> | |||
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'''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EQ1 is a [ | 1EQ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ1 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11818551 11818551] | ||
[[Category: Manduca sexta]] | [[Category: Manduca sexta]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Sykes, B D.]] | [[Category: Sykes, B D.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: | [[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 Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:58:55 2008'' | ||
Revision as of 11:58, 20 March 2008
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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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