This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 13: | Line 13: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 12:30:23 2008
