1a18

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(New page: 200px<br /><applet load="1a18" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a18, resolution 2.4&Aring;" /> '''PHENANTHROLINE MODIFI...)
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[[Image:1a18.jpg|left|200px]]<br /><applet load="1a18" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1a18, resolution 2.4&Aring;" />
 
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'''PHENANTHROLINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN'''<br />
 
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==Overview==
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==PHENANTHROLINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN==
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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.
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<StructureSection load='1a18' size='340' side='right'caption='[[1a18]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/1a18_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1A18 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A18 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9680187 9680187]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1a18" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Banaszak, L.]]
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[[Category: Davies, R.]]
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[[Category: Distefano, M.]]
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[[Category: Kuang, H.]]
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[[Category: Mazhary, A.]]
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[[Category: Ory, J.]]
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[[Category: fatty acid binding protein]]
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[[Category: phosphorylation]]
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[[Category: transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:32:42 2007''
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==See Also==
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*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Banaszak L]]
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[[Category: Davies R]]
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[[Category: Distefano M]]
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[[Category: Kuang H]]
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[[Category: Mazhary A]]
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[[Category: Ory J]]

Current revision

PHENANTHROLINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN

PDB ID 1a18

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