Related ArticlesThe sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
Biochemistry. 1997 Feb 18;36(7):1719-29
Authors: Stolowich NJ, Frolov A, Atshaves B, Murphy EJ, Jolly CA, Billheimer JT, Scott AI, Schroeder F
The interaction and orientation of fatty acids with recombinant human sterol carrier protein-2 (SCP-2) were examined by nuclear magnetic resonance (NMR), circular dichroism (CD), and fluorescence techniques. 13C-NMR spectroscopy of stearic acid and oleic acid as well as fluorescence spectroscopy of cis-parinaric acid demonstrated that SCP-2 bound naturally occurring fatty acids with near 1:1 stoichiometry. Several findings indicated that the fatty acid was oriented in the binding site with its methyl end buried in the protein interior and its carboxylate exposed at the surface: the chemical shift of bound [18-13C]-stearate; dicarboxylic/monocarboxylic acid cis-parinaric acid displacement; complete ionization of the carboxylate group of SCP-2 bound [1-13C]stearate at neutral pH; lack of electrostatic interactions between 13C-fatty acids with SCP-2 cationic residues: pH titratability of the SCP-2 bound [1-13C]stearate carboxylate group. SCP-2 did not undergo global structural changes upon ligand binding or pH decrease as indicated by the absence of significant changes in NMR and only small alterations in time resolved fluorescence parameters. However, SCP-2 did undergo secondary structural changes detected by CD in the pH range 5-6. While these changes in secondary structure did not alter the fatty acid:SCP-2 binding stoichiometry, the affinity for fatty acid was increased severalfold at lower pH. In summary, 13C-NMR, CD, and fluorescence spectroscopy provided a detailed understanding of the interaction of fatty acids with SCP-2 and further showed for the first time the orientation of the fatty acid within the binding site. The pH-induced changes in SCP-2 secondary structure and ligand binding activity may be important to the mechanism whereby this protein interacts with membrane surfaces to enhance lipid binding/transfer.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
Biochemistry. 2011 Jan 12;
Authors: He Y, Estephan R, Yang X, Vela A, Wang H, Bernard C, Stark RE
Liver fatty acid-binding protein (LFABP) is a 14-kDa cytosolic polypeptide, differing from other family members in number of ligand binding sites, diversity of bound ligands, and transfer of fatty acid(s) to...
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01-14-2011 12:05 PM
[NMR paper] Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C
Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
Related Articles Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
Biochemistry. 2001 Oct 23;40(42):12604-11
Authors: Beringhelli T, Goldoni L, Capaldi S, Bossi A, Perduca M, Monaco HL
Two different groups of liver fatty acid-binding proteins (L-FABPs) are known: the mammalian type and the basic type. Very few members of this second group of L-FABPs have been...
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11-19-2010 08:44 PM
[NMR paper] NMR structure of the sterol carrier protein-2: implications for the biological role.
NMR structure of the sterol carrier protein-2: implications for the biological role.
Related Articles NMR structure of the sterol carrier protein-2: implications for the biological role.
J Mol Biol. 2000 Jan 21;295(3):595-603
Authors: García FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wüthrich K
The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone (15)N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for...
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11-18-2010 09:15 PM
[NMR paper] Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid
Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites.
Related Articles Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites.
J Biol Chem. 1999 Dec 10;274(50):35425-33
Authors: Stolowich N, Frolov A, Petrescu AD, Scott AI, Billheimer JT, Schroeder F
Although sterol carrier protein-2 (SCP-2) stimulates sterol transfer in vitro, almost nothing is known regarding the identity of the putative cholesterol binding site. Furthermore, the interrelationship(s)...
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11-18-2010 08:31 PM
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermo
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
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J Struct Funct Genomics. 2010 Oct 5;
Authors: Goroncy AK, Murayama K, Shirouzu M, Kuramitsu S, Kigawa T, Yokoyama S
Sterol carrier protein 2 (SCP-2), also known as nonspecific lipid transfer protein, is a ubiquitous intracellular ~13*kDa protein found in mammals, insects, plants,...
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10-06-2010 06:55 PM
[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Biochemistry. 1997 Feb 25;36(8):2278-90
Authors: Hodsdon ME, Cistola DP
The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
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08-22-2010 03:31 PM
[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Biochemistry. 1997 Feb 25;36(8):2278-90
Authors: Hodsdon ME, Cistola DP
The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
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08-22-2010 03:03 PM
[NMR paper] The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and
The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
Biochemistry. 1997 Feb 18;36(7):1719-29
Authors: Stolowich NJ, Frolov A, Atshaves B, Murphy EJ, Jolly CA, Billheimer JT, Scott AI, Schroeder F
The interaction and orientation of fatty acids...
The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and
Linear Mode
