1a18: Difference between revisions

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-[[Image:1a18.png|left|200px]]
-{{STRUCTURE_1a18|  PDB=1a18  |  SCENE=  }}
+==PHENANTHROLINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN==
+<StructureSection load='1a18' size='340' side='right'caption='[[1a18]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1a18]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A18 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NPH:CYSTEINE-METHYLENE-CARBAMOYL-1,10-PHENANTHROLINE'>NPH</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a18 OCA], [https://pdbe.org/1a18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a18 RCSB], [https://www.ebi.ac.uk/pdbsum/1a18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a18 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FABP4_MOUSE FABP4_MOUSE] Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus.<ref>PMID:12077340</ref> <ref>PMID:16574478</ref> <ref>PMID:17516629</ref>
+== Evolutionary Conservation ==
+[[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/a1/1a18_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=1a18 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Adipocyte lipid-binding protein (ALBP) is a small (14.5 kDa) 10-stranded beta-barrel protein found in mammalian fat cells. The crystal structures of various holo-forms of ALBP have been solved and show the fatty acid ligand bound in a large (approximately 400 A3) cavity isolated from bulk solvent. Examination of the cavity suggests that it would be a good site for the creation of an artificial catalyst, as numerous well defined crystal structures of ALBP are available and past studies have shown the conformation to be reasonably tolerant to modification and mutagenesis. Previous work has shown ALBP to be a good protein scaffold for exploring enantio- and stereoselective reactions; two constructs, ALBP attached to either a pyridoxamine or a phenanthroline group at C117, have been chemically characterized. Both modified proteins have been crystallized and their structures solved and refined. The X-ray models have been used to examine the origin of the chiral selectivity seen in the products. It is apparent that these covalent adducts reduce the internal cavity volume, sterically limiting substrate interactions with the reactive groups, as well as solvent access to potential intermediates in the reaction pathway.
-===PHENANTHROLINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN===
+Structural characterization of two synthetic catalysts based on adipocyte lipid-binding protein.,Ory JJ, Mazhary A, Kuang H, Davies RR, Distefano MD, Banaszak LJ Protein Eng. 1998 Apr;11(4):253-61. PMID:9680187<ref>PMID:9680187</ref>
-{{ABSTRACT_PUBMED_9680187}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1a18" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[1a18]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A18 OCA].
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:009680187</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Banaszak, L.]]
+[[Category: Banaszak L]]
-[[Category: Davies, R.]]
+[[Category: Davies R]]
-[[Category: Distefano, M.]]
+[[Category: Distefano M]]
-[[Category: Kuang, H.]]
+[[Category: Kuang H]]
-[[Category: Mazhary, A.]]
+[[Category: Mazhary A]]
-[[Category: Ory, J.]]
+[[Category: Ory J]]
-[[Category: Fatty acid binding protein]]
-[[Category: Phosphorylation]]
-[[Category: Transport]]