3akm
From Proteopedia
(Difference between revisions)
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of iFABP from human and rat with bound fluorescent fatty acid analogue== | |
| + | <StructureSection load='3akm' size='340' side='right'caption='[[3akm]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3akm]] is a 4 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=3AKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AKM FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=11D:11-({[5-(DIMETHYLAMINO)NAPHTHALEN-1-YL]SULFONYL}AMINO)UNDECANOIC+ACID'>11D</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3akm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3akm OCA], [https://pdbe.org/3akm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3akm RCSB], [https://www.ebi.ac.uk/pdbsum/3akm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3akm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FABPI_HUMAN FABPI_HUMAN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor. | ||
| - | + | ==See Also== | |
| - | + | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Homo sapiens]] | |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Laguerre AJK]] | ||
| + | [[Category: Parker MW]] | ||
| + | [[Category: Scanlon MJ]] | ||
| + | [[Category: Wielens J]] | ||
Current revision
X-ray structure of iFABP from human and rat with bound fluorescent fatty acid analogue
| |||||||||||
