1tw4: Difference between revisions

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 <StructureSection load='1tw4' size='340' side='right'caption='[[1tw4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tw4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TW4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tw4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TW4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tvq|1tvq]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene></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=1tw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tw4 OCA], [http://pdbe.org/1tw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tw4 RCSB], [http://www.ebi.ac.uk/pdbsum/1tw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tw4 ProSAT]</span></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=1tw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tw4 OCA], [https://pdbe.org/1tw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tw4 RCSB], [https://www.ebi.ac.uk/pdbsum/1tw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tw4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FABPL_CHICK FABPL_CHICK]] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Binds 2 molecules of cholate per subunit.
+[https://www.uniprot.org/uniprot/FABPL_CHICK FABPL_CHICK] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Binds 2 molecules of cholate per subunit.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1tw4 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Two paralogous groups of liver fatty acid-binding proteins (FABPs) have been described: the mammalian type liver FABPs and the basic type (Lb-FABPs) characterized in several vertebrates but not in mammals. The two groups have similar sequences and share a highly conserved three-dimensional structure, but their specificity and stoichiometry of binding are different. The crystal structure of chicken Lb-FABP complexed with cholic acid and that of the apoprotein refined to 2.0 A resolution are presented in this paper. The two forms of the protein crystallize in different space groups, and significant changes are observed between the two conformations. The holoprotein binds two molecules of cholate in the interior cavity, and the contacts observed between the two ligands can help to explain the reason for this stoichiometry of binding. Most of the amino acids involved in ligand binding are conserved in other members of the Lb-FABP family. Since the amino acid sequence of the Lb-FABPs is more similar to that of the bile acid-binding proteins than to that of the L-FABPs, the possibility that the Lb-FABPs might be more appropriately called liver bile acid-binding proteins (L-BABPs) is suggested.
-Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid.,Nichesola D, Perduca M, Capaldi S, Carrizo ME, Righetti PG, Monaco HL Biochemistry. 2004 Nov 9;43(44):14072-9. PMID:15518556<ref>PMID:15518556</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1tw4" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Capaldi, S]]
+[[Category: Capaldi S]]
-[[Category: Carrizo, M E]]
+[[Category: Carrizo ME]]
-[[Category: Monaco, H L]]
+[[Category: Monaco HL]]
-[[Category: Nichesola, D]]
+[[Category: Nichesola D]]
-[[Category: Perduca, M]]
+[[Category: Perduca M]]
-[[Category: Righetti, P G]]
+[[Category: Righetti PG]]
-[[Category: Babp]]
-[[Category: Bile acid]]
-[[Category: Cholic acid]]
-[[Category: Fabp]]
-[[Category: Intracellular bile acid-binding protein]]
-[[Category: Lb-fabp]]
-[[Category: Lipid binding protein]]