1hb6: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hb6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HB6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1hb6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HB6 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aca|1aca]], [[2abd|2abd]], [[1hb8|1hb8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aca|1aca]], [[2abd|2abd]], [[1hb8|1hb8]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hb6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hb6 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hb6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hb6 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bergfors, T | [[Category: Bergfors, T]] | ||
[[Category: Jones, T A | [[Category: Jones, T A]] | ||
[[Category: Kleywegt, G J | [[Category: Kleywegt, G J]] | ||
[[Category: Knudsen, J | [[Category: Knudsen, J]] | ||
[[Category: Zou, J Y | [[Category: Zou, J Y]] | ||
[[Category: Acyl-coa]] | [[Category: Acyl-coa]] | ||
[[Category: Acyl-coenzyme a binding protein]] | [[Category: Acyl-coenzyme a binding protein]] | ||
[[Category: Binding protein]] | [[Category: Binding protein]] | ||
Revision as of 22:37, 22 December 2014
STRUCTURE OF BOVINE ACYL-COA BINDING PROTEIN IN ORTHORHOMBIC CRYSTAL FORMSTRUCTURE OF BOVINE ACYL-COA BINDING PROTEIN IN ORTHORHOMBIC CRYSTAL FORM
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAcyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 A resolution crystal structures of a P. falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures published previously; however, the bovine and parasite ACBP structures are less similar. The parasite ACBP is shown to have a different ligand-binding pocket, leading to an acyl-CoA binding specificity different from that of bovine ACBP. Several non-conservative differences in residues that interact with the ligand were identified between the mammalian and parasite ACBPs. These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site. Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein.,van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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