1eq1
From Proteopedia
(New page: 200px<br /><applet load="1eq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eq1" /> '''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROT...) |
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| - | [[Image:1eq1.gif|left|200px]]<br /><applet load="1eq1" size=" | + | [[Image:1eq1.gif|left|200px]]<br /><applet load="1eq1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1eq1" /> | caption="1eq1" /> | ||
'''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III'''<br /> | '''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The high-resolution NMR structure of apolipophorin III from the sphinx | + | 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 Structure== | ==About this Structure== | ||
| - | 1EQ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta]. Full crystallographic information is available from [http:// | + | 1EQ1 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Manduca sexta]] | [[Category: Manduca sexta]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ryan, R | + | [[Category: Ryan, R O.]] |
| - | [[Category: Sykes, B | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:23 2008'' |
Revision as of 10:30, 21 February 2008
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NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III
Overview
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 Structure
1EQ1 is a Single protein structure of sequence from Manduca sexta. Full crystallographic information is available from OCA.
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:11818551
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