4tkb: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4tkb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TKB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</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]] 0.86&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</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=4tkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkb OCA], [https://pdbe.org/4tkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tkb RCSB], [https://www.ebi.ac.uk/pdbsum/4tkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tkb ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/FABPH_HUMAN FABPH_HUMAN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Long-chain fatty acids (FAs) with low water solubility require fatty-acid-binding proteins (FABPs) to transport them from cytoplasm to the mitochondria for energy production. However, the precise mechanism by which these proteins recognize the various lengths of simple alkyl chains of FAs with similar high affinity remains unknown. To address this question, we employed a newly developed calorimetric method for comprehensively evaluating the affinity of FAs, sub-Angstrom X-ray crystallography to accurately determine their 3D structure, and energy calculations of the coexisting water molecules using the computer program WaterMap. Our results clearly showed that the heart-type FABP (FABP3) preferentially incorporates a U-shaped FA of C10-C18 using a lipid-compatible water cluster, and excludes longer FAs using a chain-length-limiting water cluster. These mechanisms could help us gain a general understanding of how proteins recognize diverse lipids with different chain lengths.
-Water-mediated recognition of simple alkyl chains by heart-type Fatty-Acid-binding protein.,Matsuoka S, Sugiyama S, Matsuoka D, Hirose M, Lethu S, Ano H, Hara T, Ichihara O, Kimura SR, Murakami S, Ishida H, Mizohata E, Inoue T, Murata M Angew Chem Int Ed Engl. 2015 Jan 26;54(5):1508-11. doi: 10.1002/anie.201409830., Epub 2014 Dec 9. PMID:25491543<ref>PMID:25491543</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4tkb" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>