Role of Buried Polar Residues in Helix Bundle Stability and Lipid Binding of Apolipophorin III:  Destabilization by Threonine 31†

Biochemistry ◽  
2005 ◽  
Vol 44 (24) ◽  
pp. 8810-8816 ◽  
Author(s):  
Paul M. M. Weers ◽  
Wazir E. Abdullahi ◽  
Jamie M. Cabrera ◽  
Tzu-Chi Hsu
Keyword(s):  
Lipid Binding ◽  
Helix Bundle ◽  
Apolipophorin Iii ◽  
Polar Residues

scholarly journals Role of the N- and C-Terminal Helices in Apolipophorin III Stability and Lipid Binding

2012 ◽  
Vol 102 (3) ◽  
pp. 58a
Author(s):  
Pankaj Dwivedi ◽  
Johana Rodriguez ◽  
Paul M.M. Weers
Keyword(s):  
Lipid Binding ◽  
Apolipophorin Iii

Role of charged amino acid side chains in the stability and lipid binding ofManduca sexta apolipophorin III

1995 ◽  
Vol 30 (2-3) ◽  
pp. 211-223 ◽  
Author(s):  
Minal Upadhyaya ◽  
Kim Oikawa ◽  
Cyril M. Kay ◽  
Douglas G. Scraba ◽  
Roger Bradley ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lipid Binding ◽  
Side Chains ◽  
Apolipophorin Iii ◽  
Amino Acid Side Chains ◽  
The Stability

Abstract 391: Apolipoprotein E3, Apolipoprotein AI, and Apolipophorin III Chimeras Provide Insight Into the Domain Organization of Apolipoproteins

2016 ◽  
Vol 36 (suppl_1) ◽  
Author(s):  
James V Horn ◽  
Mark Lek ◽  
Nnejiuwa Ibe ◽  
Rachel A Ellena ◽  
Wendy H Beck ◽  
...  
Keyword(s):  
Cholesterol Efflux ◽  
Dominant Role ◽  
Lipoprotein Metabolism ◽  
Lipid Binding ◽  
Binding Activity ◽  
Domain Model ◽  
Helix Bundle ◽  
Apolipophorin Iii ◽  
Helical Content ◽  
The Stability

Apolipoproteins (apo) A-I and E are exchangeable apolipoproteins that play a dominant role in regulating lipoprotein metabolism. They are composed of a series of amphipathic α-helices, which are organized into an N-terminal (NT) helix bundle domain and a smaller C-terminal (CT) domain. The objective of the current study is to understand the functional and structural role of the domains of these proteins by “domain swapping” using apoE3 and apoAI, both of which bear a 4-helix bundle in their NT domain, and apolipophorin III (apoLp-III), a monomeric one-domain model apolipoprotein. A series of chimeric apolipoproteins were generate: apoE3-NT/apoAI-CT, apoAI-NT/apoE-CT and apoLp-III/apoA-I-CT. The α-helical content of the chimeras was comparable to that of the parent proteins. Unfolding studies indicated that addition of CT-apoE3 to NT-apoAI conferred more stability to apoAI. While addition of CT-apoAI to NT-apoE3 had no significant effect on the stability of apoE3, addition of NT-apoAI to apoLp-III increased the stability of apoLp-III. Moreover, apoLp-III switched from a monomeric to an oligomeric protein upon addition of CT-apoAI, showing that CT-apoAI has a strong tendency to self-associate. Addition of CT-apoAI to NT-apoE or apoLp-III increased the lipid binding activity by ~ 10-fold, while addition of apoE-CT to apoA-I-NT had no measurable effect on the lipid binding activity. All three chimeras promote ABCA1-mediated cholesterol efflux from J774 macrophages, with the efflux capability being highest for apoAI-NT/apoE-CT. Whereas apoE3-NT/apoAI-CT elicits LDLr binding ability, apoAI-NT/apoE-CT did not. These results suggest that CT of apoAI is a strong promoter of lipid binding, while CT of apoE3 can improve cholesterol efflux ability of apoAI.

scholarly journals Essential Role of the Conformational Flexibility of Helices 1 and 5 on the Lipid Binding Activity of Apolipophorin-III

2001 ◽  
Vol 276 (36) ◽  
pp. 34162-34166 ◽  
Author(s):  
Jose L. Soulages ◽  
Estela L. Arrese ◽  
Palaniappan S. Chetty ◽  
Veronica Rodriguez
Keyword(s):  
Essential Role ◽  
Conformational Flexibility ◽  
Lipid Binding ◽  
Binding Activity ◽  
Apolipophorin Iii

The role of dynamics in modulating ligand exchange in intracellular lipid binding proteins

2014 ◽  
Vol 1844 (7) ◽  
pp. 1268-1278 ◽  
Author(s):  
Laura Ragona ◽  
Katiuscia Pagano ◽  
Simona Tomaselli ◽  
Filippo Favretto ◽  
Alberto Ceccon ◽  
...  
Keyword(s):  
Ligand Exchange ◽  
Binding Proteins ◽  
Lipid Binding ◽  
Intracellular Lipid ◽  
Lipid Binding Proteins

scholarly journals An insect lipoprotein hybrid helps to define the role of apolipophorin III.

1988 ◽  
Vol 263 (4) ◽  
pp. 2027-2033
Author(s):  
D J Van der Horst ◽  
R O Ryan ◽  
M C Van Heusden ◽  
T K Schulz ◽  
J M Van Doorn ◽  
...  
Keyword(s):  
Apolipophorin Iii

scholarly journals The role of apolipoprotein AI domains in lipid binding

1996 ◽  
Vol 93 (24) ◽  
pp. 13605-13610 ◽  
Author(s):  
W. S. Davidson ◽  
T. Hazlett ◽  
W. W. Mantulin ◽  
A. Jonas
Keyword(s):  
Lipid Binding ◽  
Apolipoprotein Ai

scholarly journals Cryo-EM structures of the DCPIB-inhibited volume-regulated anion channel LRRC8A in lipid nanodiscs

2018 ◽  
Author(s):  
David M. Kern ◽  
SeCheol Oh ◽  
Richard K. Hite ◽  
Stephen G. Brohawn
Keyword(s):  
Lipid Bilayers ◽  
Critical Role ◽  
Anion Channel ◽  
Lipid Binding ◽  
Channel Structure ◽  
Anion Channels ◽  
Cryo Electron Microscopy ◽  
Lipid Nanodiscs ◽  
Insight Into

AbstractHypoosmotic conditions activate volume-regulated anion channels in vertebrate cells. These channels are formed by leucine-rich repeat-containing protein 8 (LRRC8) family members and contain LRRC8A in homo- or hetero-hexameric assemblies. Here we present single-particle cryo-electron microscopy structures of LRRC8A in complex with the inhibitor DCPIB reconstituted in lipid nanodiscs. DCPIB plugs the channel like a cork in a bottle - binding in the extracellular selectivity filter and sterically occluding ion conduction. Constricted and expanded structures reveal coupled dilation of cytoplasmic LRRs and the channel pore, suggesting a mechanism for channel gating by internal stimuli. Conformational and symmetry differences between LRRC8A structures determined in detergent micelles and lipid bilayers related to reorganization of intersubunit lipid binding sites demonstrate a critical role for the membrane in determining channel structure. These results provide insight into LRRC8 gating and inhibition and the role of lipids in the structure of an ionic-strength sensing ion channel.

Sign in / Sign up

Export Citation Format

Share Document