1a2d

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[[Image:1a2d.gif|left|200px]]
 
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{{Structure
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==PYRIDOXAMINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN==
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|PDB= 1a2d |SIZE=350|CAPTION= <scene name='initialview01'>1a2d</scene>, resolution 2.4&Aring;
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<StructureSection load='1a2d' size='340' side='right'caption='[[1a2d]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PYX:S-[S-THIOPYRIDOXAMINYL]CYSTEINE'>PYX</scene>
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<table><tr><td colspan='2'>[[1a2d]] is a 2 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=1A2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2D FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PYX:S-[S-THIOPYRIDOXAMINYL]CYSTEINE'>PYX</scene></td></tr>
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|DOMAIN=
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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=1a2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2d OCA], [https://pdbe.org/1a2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2d RCSB], [https://www.ebi.ac.uk/pdbsum/1a2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2d ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2d OCA], [http://www.ebi.ac.uk/pdbsum/1a2d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a2d RCSB]</span>
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== Function ==
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}}
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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/a2/1a2d_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=1a2d 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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'''PYRIDOXAMINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1a2d" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1A2D is a [[Single protein]] structure of 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=1A2D OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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://www.ncbi.nlm.nih.gov/pubmed/9680187 9680187]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Banaszak L]]
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[[Category: Banaszak, L.]]
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[[Category: Davies R]]
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[[Category: Davies, R.]]
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[[Category: Distefano M]]
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[[Category: Distefano, M.]]
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[[Category: Kuang H]]
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[[Category: Kuang, H.]]
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[[Category: Mazhary A]]
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[[Category: Mazhary, A.]]
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[[Category: Ory J]]
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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://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:31:35 2008''
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Current revision

PYRIDOXAMINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN

PDB ID 1a2d

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