3vg3: Difference between revisions
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==Cadmium derivative of human LFABP== | ==Cadmium derivative of human LFABP== | ||
<StructureSection load='3vg3' size='340' side='right' caption='[[3vg3]], [[Resolution|resolution]] 2.22Å' scene=''> | <StructureSection load='3vg3' size='340' side='right'caption='[[3vg3]], [[Resolution|resolution]] 2.22Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vg3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3vg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VG3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b2h|3b2h]], [[3b2i|3b2i]], [[3b2j|3b2j]], [[3b2k|3b2k]], [[3b2l|3b2l]], [[3vg2|3vg2]], [[3vg4|3vg4]], [[3vg5|3vg5]], [[3vg6|3vg6]], [[3vg7|3vg7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3b2h|3b2h]], [[3b2i|3b2i]], [[3b2j|3b2j]], [[3b2k|3b2k]], [[3b2l|3b2l]], [[3vg2|3vg2]], [[3vg4|3vg4]], [[3vg5|3vg5]], [[3vg6|3vg6]], [[3vg7|3vg7]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABP1, FABPL ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABP1, FABPL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vg3 OCA], [https://pdbe.org/3vg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vg3 RCSB], [https://www.ebi.ac.uk/pdbsum/3vg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vg3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/FABPL_HUMAN FABPL_HUMAN]] 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
==See Also== | ==See Also== | ||
*[[Fatty acid-binding protein|Fatty acid-binding protein]] | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 28: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Sharma, A]] | [[Category: Sharma, A]] | ||
[[Category: Yogavel, M]] | [[Category: Yogavel, M]] | ||
Revision as of 21:43, 27 July 2022
Cadmium derivative of human LFABPCadmium derivative of human LFABP
Structural highlights
Function[FABPL_HUMAN] 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. Publication Abstract from PubMedWe report the use of anionic (I(-)), cationic (Ba(2+), Cd(2+)) and ionic mixtures (I(-) plus Ba(2+)) for derivatizing liver fatty acid binding protein (LFABP) crystals. Use of cationic and anionic salts in phasing experiments revealed distinct non-overlapping sites for these ions, suggesting exclusive binding regions on LFABP. Interestingly, cations of identical charge and valency (like Ba(2+) and Cd(2+)) bound to distinct pockets on the protein surface. Furthermore, a mixture of salts containing both I(-) and Ba(2+) was very useful in phasing experiments as these oppositely charged ions bound to different regions of LFABP. Our data therefore suggest that cationic and anionic salt mixtures like BaCl(2) with NH(4)I or salts like CdI, BaI where each ion has a significant anomalous signal for a given X-ray wavelength may be valuable reagents for phasing during structure determination. Utility of anion and cation combinations for phasing of protein structures.,Sharma A, Yogavel M, Sharma A J Struct Funct Genomics. 2012 May 6. PMID:22562242[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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