1hb6: Difference between revisions

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-[[Image:1hb6.jpg|left|200px]]
-<!--
+==Structure of bovine Acyl-CoA binding protein in orthorhombic crystal form==
-The line below this paragraph, containing "STRUCTURE_1hb6", creates the "Structure Box" on the page.
+<StructureSection load='1hb6' size='340' side='right'caption='[[1hb6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1hb6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1HB6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
-{{STRUCTURE_1hb6|  PDB=1hb6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb6 OCA], [https://pdbe.org/1hb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hb6 RCSB], [https://www.ebi.ac.uk/pdbsum/1hb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hb6 ProSAT]</span></td></tr>
+</table>
-'''STRUCTURE OF BOVINE ACYL-COA BINDING PROTEIN IN ORTHORHOMBIC CRYSTAL FORM'''
+== Function ==
+[https://www.uniprot.org/uniprot/ACBP_BOVIN ACBP_BOVIN] Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.<ref>PMID:11491287</ref>
+== Evolutionary Conservation ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hb/1hb6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hb6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
 Acyl-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.
-==About this Structure==
+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<ref>PMID:11491287</ref>
-HB6 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB6 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://www.ncbi.nlm.nih.gov/pubmed/11491287 11491287]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1hb6" style="background-color:#fffaf0;"></div>
-[[Category: Bergfors, T.]]
+== References ==
-[[Category: Jones, T A.]]
+<references/>
-[[Category: Kleywegt, G J.]]
+__TOC__
-[[Category: Knudsen, J.]]
+</StructureSection>
-[[Category: Zou, J Y.]]
+[[Category: Bos taurus]]
-[[Category: Acyl-coa]]
+[[Category: Large Structures]]
-[[Category: Binding protein]]
+[[Category: Bergfors T]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:39:41 2008''
+[[Category: Jones TA]]
+[[Category: Kleywegt GJ]]
+[[Category: Knudsen J]]
+[[Category: Zou JY]]