4wbk
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wbk]] 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=4WBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WBK FirstGlance]. <br> | <table><tr><td colspan='2'>[[4wbk]] 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=4WBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WBK FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=STE:STEARIC+ACID'>STE</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]] 1.37Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=STE:STEARIC+ACID'>STE</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=4wbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wbk OCA], [https://pdbe.org/4wbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wbk RCSB], [https://www.ebi.ac.uk/pdbsum/4wbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wbk 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=4wbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wbk OCA], [https://pdbe.org/4wbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wbk RCSB], [https://www.ebi.ac.uk/pdbsum/4wbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wbk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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. | [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 == | ||
| - | Intracellular lipid binding proteins (iLBPs) share distinctive features: a rigid protein structure composed of a beta-barrel and an alpha-helix cap, and a large internalized water cluster. Although X-ray crystallographic studies have elucidated the three-dimensional structures of iLBPs, the protein dynamics and the role of the large water cluster in protein function remain unknown. In the present study, we performed molecular dynamics (MD) simulations on human heart-type fatty acid binding protein (FABP3), a typical iLBP that is highly expressed in heart and skeletal muscles, and showed that an altered mode of protein dynamics and rearrangement of the internal water cluster are key elements of ligand binding. Using simulations without a ligand at 310 K, we first demonstrated that FABP3 adopts a wide-open conformation, achieved by a combination of two modes of dynamics: portal opening by a domain motion of the alpha-helices and gap opening by cleavage of the hydrogen-bond network between betaD and betaE strands. In contrast, stearic acid-bound FABP3 mainly adopted a closed form, stabilized by the H-bond network inside the binding cavity, which latches the gap, and by protein-ligand hydrophobic interactions. The wide-open apo FABP3 represents a biologically important conformation relevant to ligand loading. | ||
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| - | Molecular Dynamics Simulations of Heart-type Fatty Acid Binding Protein in Apo and Holo Forms, and Hydration Structure Analyses in the Binding Cavity.,Matsuoka D, Sugiyama S, Murata M, Matsuoka S J Phys Chem B. 2015 Jan 8;119(1):114-27. doi: 10.1021/jp510384f. Epub 2014 Dec, 22. PMID:25489786<ref>PMID:25489786</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4wbk" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
The 1.37 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with stearic acid
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Categories: Homo sapiens | Large Structures | Inoue T | Matsuoka D | Matsuoka S | Mizohata E | Murakami S | Murata M | Sugiyama S
