1mvg

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(New page: 200px<br /><applet load="1mvg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mvg" /> '''NMR solution structure of chicken Liver basi...)
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[[Image:1mvg.gif|left|200px]]<br /><applet load="1mvg" size="350" color="white" frame="true" align="right" spinBox="true"
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'''NMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)'''<br />
'''NMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)'''<br />
==Overview==
==Overview==
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Chicken liver basic fatty acid binding protein (Lb-FABP) belongs to the, basic-type fatty acid binding proteins, a novel group of proteins isolated, from liver of different non mammalian species whose structure is not, known. The structure of Lb-FABP has been solved by (1)H NMR. The overall, fold of Lb-FABP, common to the other proteins of the family, consists of, ten antiparallel beta-strands organised in two nearly ortogonal, beta-sheets with two alpha helices closing the protein cavity where small, hydrophobic ligands can be bound. The binding specificity of the protein, is not known, however, based on the high sequence and structural, similarity with an orthologous protein, ileal lipid binding protein, it is, suggested that bile acids may be the putative ligands.
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Chicken liver basic fatty acid binding protein (Lb-FABP) belongs to the basic-type fatty acid binding proteins, a novel group of proteins isolated from liver of different non mammalian species whose structure is not known. The structure of Lb-FABP has been solved by (1)H NMR. The overall fold of Lb-FABP, common to the other proteins of the family, consists of ten antiparallel beta-strands organised in two nearly ortogonal beta-sheets with two alpha helices closing the protein cavity where small hydrophobic ligands can be bound. The binding specificity of the protein is not known, however, based on the high sequence and structural similarity with an orthologous protein, ileal lipid binding protein, it is suggested that bile acids may be the putative ligands.
==About this Structure==
==About this Structure==
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1MVG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MVG OCA].
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1MVG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVG OCA].
==Reference==
==Reference==
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[[Category: ten antiparallel beta strands]]
[[Category: ten antiparallel beta strands]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:43:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:24 2008''

Revision as of 11:59, 21 February 2008


1mvg

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NMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)

Overview

Chicken liver basic fatty acid binding protein (Lb-FABP) belongs to the basic-type fatty acid binding proteins, a novel group of proteins isolated from liver of different non mammalian species whose structure is not known. The structure of Lb-FABP has been solved by (1)H NMR. The overall fold of Lb-FABP, common to the other proteins of the family, consists of ten antiparallel beta-strands organised in two nearly ortogonal beta-sheets with two alpha helices closing the protein cavity where small hydrophobic ligands can be bound. The binding specificity of the protein is not known, however, based on the high sequence and structural similarity with an orthologous protein, ileal lipid binding protein, it is suggested that bile acids may be the putative ligands.

About this Structure

1MVG is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Solution structure of chicken liver basic fatty acid binding protein., Vasile F, Ragona L, Catalano M, Zetta L, Perduca M, Monaco H, Molinari H, J Biomol NMR. 2003 Feb;25(2):157-60. PMID:12652125

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