1tw4: Difference between revisions
New page: left|200px<br /><applet load="1tw4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tw4, resolution 2.00Å" /> '''Crystal Structure of... |
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[[Image:1tw4.gif|left|200px]]<br /><applet load="1tw4" size=" | [[Image:1tw4.gif|left|200px]]<br /><applet load="1tw4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1tw4, resolution 2.00Å" /> | caption="1tw4, resolution 2.00Å" /> | ||
'''Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid'''<br /> | '''Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid'''<br /> | ||
==Overview== | ==Overview== | ||
Two paralogous groups of liver fatty acid-binding proteins (FABPs) have | Two paralogous groups of liver fatty acid-binding proteins (FABPs) have been described: the mammalian type liver FABPs and the basic type (Lb-FABPs) characterized in several vertebrates but not in mammals. The two groups have similar sequences and share a highly conserved three-dimensional structure, but their specificity and stoichiometry of binding are different. The crystal structure of chicken Lb-FABP complexed with cholic acid and that of the apoprotein refined to 2.0 A resolution are presented in this paper. The two forms of the protein crystallize in different space groups, and significant changes are observed between the two conformations. The holoprotein binds two molecules of cholate in the interior cavity, and the contacts observed between the two ligands can help to explain the reason for this stoichiometry of binding. Most of the amino acids involved in ligand binding are conserved in other members of the Lb-FABP family. Since the amino acid sequence of the Lb-FABPs is more similar to that of the bile acid-binding proteins than to that of the L-FABPs, the possibility that the Lb-FABPs might be more appropriately called liver bile acid-binding proteins (L-BABPs) is suggested. | ||
==About this Structure== | ==About this Structure== | ||
1TW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CHD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1TW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CHD:'>CHD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TW4 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Capaldi, S.]] | [[Category: Capaldi, S.]] | ||
[[Category: Carrizo, M | [[Category: Carrizo, M E.]] | ||
[[Category: Monaco, H | [[Category: Monaco, H L.]] | ||
[[Category: Nichesola, D.]] | [[Category: Nichesola, D.]] | ||
[[Category: Perduca, M.]] | [[Category: Perduca, M.]] | ||
[[Category: Righetti, P | [[Category: Righetti, P G.]] | ||
[[Category: CHD]] | [[Category: CHD]] | ||
[[Category: babp]] | [[Category: babp]] | ||
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[[Category: lb-fabp]] | [[Category: lb-fabp]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:58 2008'' | ||
Revision as of 16:18, 21 February 2008
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Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid
OverviewOverview
Two paralogous groups of liver fatty acid-binding proteins (FABPs) have been described: the mammalian type liver FABPs and the basic type (Lb-FABPs) characterized in several vertebrates but not in mammals. The two groups have similar sequences and share a highly conserved three-dimensional structure, but their specificity and stoichiometry of binding are different. The crystal structure of chicken Lb-FABP complexed with cholic acid and that of the apoprotein refined to 2.0 A resolution are presented in this paper. The two forms of the protein crystallize in different space groups, and significant changes are observed between the two conformations. The holoprotein binds two molecules of cholate in the interior cavity, and the contacts observed between the two ligands can help to explain the reason for this stoichiometry of binding. Most of the amino acids involved in ligand binding are conserved in other members of the Lb-FABP family. Since the amino acid sequence of the Lb-FABPs is more similar to that of the bile acid-binding proteins than to that of the L-FABPs, the possibility that the Lb-FABPs might be more appropriately called liver bile acid-binding proteins (L-BABPs) is suggested.
About this StructureAbout this Structure
1TW4 is a Single protein structure of sequence from Gallus gallus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid., Nichesola D, Perduca M, Capaldi S, Carrizo ME, Righetti PG, Monaco HL, Biochemistry. 2004 Nov 9;43(44):14072-9. PMID:15518556
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