1eq1: Difference between revisions

Revision as of 01:36, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1eq1.png

Template:STRUCTURE 1eq1

NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-IIINMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III

Template:ABSTRACT PUBMED 11818551

About this StructureAbout this Structure

1EQ1 is a Single protein structure of sequence from Manduca sexta. Full experimental 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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OCA

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-'''NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11818551}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11818551 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11818551}}
 ==About this Structure==
-EQ1 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].
+EQ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ1 OCA].
 ==Reference==
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 [[Category: Helix-short helix-helix recognition motif]]
 [[Category: Five helix-bundle]]
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