1alb: Difference between revisions

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 <StructureSection load='1alb' size='340' side='right'caption='[[1alb]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1alb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1alb]] 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=1ALB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALB FirstGlance]. <br>
-</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=1alb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alb OCA], [https://pdbe.org/1alb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alb RCSB], [https://www.ebi.ac.uk/pdbsum/1alb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alb ProSAT]</span></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]] 2.5&#8491;</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=1alb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alb OCA], [https://pdbe.org/1alb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alb RCSB], [https://www.ebi.ac.uk/pdbsum/1alb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alb 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>
+[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]]
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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=1alb ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Adipocyte lipid-binding protein (ALBP) is the adipocyte member of an intracellular hydrophobic ligand-binding protein family. ALBP is phosphorylated by the insulin receptor kinase upon insulin stimulation. The crystal structure of recombinant murine ALBP has been determined and refined to 2.5 A. The final R factor for the model is 0.18 with good canonical properties. Crystalline ALBP has a conformation which is essentially identical to that of intestinal fatty acid binding protein and myelin P2 protein. Although the crystal structure is of the apo- form, a cavity resembling that in other family members is present. It contains a number of bound and implied unbound water molecules and shows no large obvious portal to the external milieu. The cavity of ALBP, which by homology is the ligand-binding site, is formed by both polar and hydrophobic residues among which is tyrosine 19. Y19 is phosphorylated by the insulin receptor kinase as described in the accompanying paper [Buelt, M. K., Xu, Z., Banaszak, L. J., &amp; Bernlohr, D. A. (1992) Biochemistry (following paper in this issue)]. By comparing ALBP with the earlier structural results on intestinal fatty acid binding protein, it is now possible to delineate conserved amino acids which help form the binding site in this family.
-Crystal structure of recombinant murine adipocyte lipid-binding protein.,Xu Z, Bernlohr DA, Banaszak LJ Biochemistry. 1992 Apr 7;31(13):3484-92. PMID:1554730<ref>PMID:1554730</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1alb" style="background-color:#fffaf0;"></div>
 ==See Also==
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 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Banaszak, L J]]
+[[Category: Banaszak LJ]]
-[[Category: Xu, Z]]
+[[Category: Xu Z]]
-[[Category: Lipid binding protein]]
-[[Category: Lipid-binding protein]]