1eq1: Difference between revisions

Revision as of 13:30, 21 February 2008

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 Thu Feb 21 12:30:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1eq1.gif|left|200px]]<br /><applet load="1eq1" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1eq1" />
 '''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III'''<br />
 ==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.
+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==
-EQ1 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EQ1 OCA].
+EQ1 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==
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 [[Category: Manduca sexta]]
 [[Category: Single protein]]
-[[Category: Ryan, R.O.]]
+[[Category: Ryan, R O.]]
-[[Category: Sykes, B.D.]]
+[[Category: Sykes, B D.]]
 [[Category: Wang, J.]]
 [[Category: "helix-short helix-helix" recognition motif]]
 [[Category: five helix-bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:13:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:23 2008''