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| | ==Solution structure of Human Intestinal Fatty acid binding protein== | | ==Solution structure of Human Intestinal Fatty acid binding protein== |
| - | <StructureSection load='1kzw' size='340' side='right'caption='[[1kzw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1kzw' size='340' side='right'caption='[[1kzw]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kzw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KZW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kzw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KZW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kzx|1kzx]], [[3ifb|3ifb]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABP2 ([http://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'>[https://proteopedia.org/fgij/fg.htm?mol=1kzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzw OCA], [https://pdbe.org/1kzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kzw RCSB], [https://www.ebi.ac.uk/pdbsum/1kzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kzw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzw OCA], [http://pdbe.org/1kzw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kzw RCSB], [http://www.ebi.ac.uk/pdbsum/1kzw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kzw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baier, L J]] | + | [[Category: Baier LJ]] |
| - | [[Category: Hamilton, J A]] | + | [[Category: Hamilton JA]] |
| - | [[Category: Luecke, C]] | + | [[Category: Luecke C]] |
| - | [[Category: Sacchettini, J C]] | + | [[Category: Sacchettini JC]] |
| - | [[Category: Zhang, F]] | + | [[Category: Zhang F]] |
| - | [[Category: 15n isotope labelling]]
| + | |
| - | [[Category: Fatty acid binding]]
| + | |
| - | [[Category: Holo-form]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Nmr spectroscopy]]
| + | |
| - | [[Category: Single base polymorphism]]
| + | |
| - | [[Category: Type 2 diabetes]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The human intestinal fatty acid binding protein (I-FABP) belongs to a family of intracellular lipid binding proteins. This 15 kDa protein binds dietary long-chain fatty acids in the cytosol of enterocytes. A naturally-occurring nucleotide polymorphism at codon 54, which produces either an alanine-containing (A54) or a threonine-containing (T54) protein, has been identified. These two I-FABP forms display differential binding and transport of fatty acids across cells, and their alleles are associated with in vivo insulin resistance and/or altered lipid metabolism in several human populations. The three-dimensional solution structure of the more common A54 form was previously determined in our lab. A direct comparison between human A54 and T54 I-FABP has now been performed to help elucidate the structural origins of their physiological distinctions. The solution structure of T54 I-FABP is highly homologous to that of A54 I-FABP, with the same overall three-dimensional fold that includes an antiparallel beta-clam motif. Chemical shift differences between the two proteins suggest only minor local structural changes within the "portal region" and no significant alterations elsewhere. Hence, the slightly stronger binding of fatty acids to T54 I-FABP does not originate from residues in direct contact with the bound fatty acid. Instead, it appears that the larger Thr(54) side chain affects the passage of the ligand through the entry portal. Structural details of this portal region will be discussed in view of the influence residue 54 exerts on the functional properties of human I-FABP.
Solution structure of human intestinal fatty acid binding protein with a naturally-occurring single amino acid substitution (A54T) that is associated with altered lipid metabolism.,Zhang F, Lucke C, Baier LJ, Sacchettini JC, Hamilton JA Biochemistry. 2003 Jun 24;42(24):7339-47. PMID:12809489[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang F, Lucke C, Baier LJ, Sacchettini JC, Hamilton JA. Solution structure of human intestinal fatty acid binding protein with a naturally-occurring single amino acid substitution (A54T) that is associated with altered lipid metabolism. Biochemistry. 2003 Jun 24;42(24):7339-47. PMID:12809489 doi:10.1021/bi0273617
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