Fatty acid-binding protein
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='1fe3' size='350' side='right' scene='48/487562/Cv/ | + | <StructureSection load='1fe3' size='350' side='right' scene='48/487562/Cv/3' caption='Human brain-type fatty acid-binding protein complex with oleate (PDB code [[1fe3]]) '> |
'''Fatty acid-binding protein''' (FABP) are carrier proteins for fatty acids and other lipophilic substances. They facilitate the transfer of fatty acids between extra- and intracellular membranes. FABS coordinate lipid trafficking and signaling in cells<ref>PMID:16424607</ref>. Various FABS differ in their tissue expression. '''IFABP''' is intestinal; '''HFABP''' is heart-type; '''BFABP''' is brain-type; '''LFABP''' is liver-type; '''AFABP''' is adipocyte; '''LMDABP''' is from flight muscle; '''TFABP''' is from testis; '''EXFABP''' is extracellular. | '''Fatty acid-binding protein''' (FABP) are carrier proteins for fatty acids and other lipophilic substances. They facilitate the transfer of fatty acids between extra- and intracellular membranes. FABS coordinate lipid trafficking and signaling in cells<ref>PMID:16424607</ref>. Various FABS differ in their tissue expression. '''IFABP''' is intestinal; '''HFABP''' is heart-type; '''BFABP''' is brain-type; '''LFABP''' is liver-type; '''AFABP''' is adipocyte; '''LMDABP''' is from flight muscle; '''TFABP''' is from testis; '''EXFABP''' is extracellular. | ||
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== Structural insights == | == Structural insights == | ||
| - | The <scene name='48/487562/Cv/2'>FABP active site binds fatty acids</scene><ref>PMID:10854433</ref>. | + | The <scene name='48/487562/Cv/2'>FABP active site binds fatty acids</scene> ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}})<ref>PMID:10854433</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 12:12, 25 January 2016
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3D structures of fatty acid-binding protein
Updated on 25-January-2016
References
- ↑ Chmurzynska A. The multigene family of fatty acid-binding proteins (FABPs): function, structure and polymorphism. J Appl Genet. 2006;47(1):39-48. PMID:16424607 doi:http://dx.doi.org/10.1007/BF03194597
- ↑ Balendiran GK, Schnutgen F, Scapin G, Borchers T, Xhong N, Lim K, Godbout R, Spener F, Sacchettini JC. Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein. J Biol Chem. 2000 Sep 1;275(35):27045-54. PMID:10854433 doi:10.1074/jbc.M003001200
