3v2p | pdb_00003v2p

COMPcc in complex with fatty acids

spinqualitylabelsall models 3v2p, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3v2p is a 5 chain structure with sequence from Bacteroides caccae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: STE Related: 1mz9, 3v2n, 3v2q, 3v2r, 3v2s Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed BACKGROUND: COMPcc forms a pentameric left-handed coiled coil that is known to bind hydrophilic signaling molecules such as vitamin D(3), and vitamin A. PRINCIPAL FINDINGS: In an integrated approach we reveal the unique binding properties of COMPcc for saturated and unsaturated fatty acids. Our observations suggest that residues Met33 (gating pore), Thr40/Asn41 (water chamber) and Gln54 (electrostatic trap) are key elements for the binding of fatty acids by COMPcc. In addition, this work characterizes the binding of various fatty acids to COMPcc using fluorescence spectroscopy. Our findings reveal a binding trend within the hydrophobic channel of COMPcc, namely, that is driven by length of the methylene tail and incorporation of unsaturation. CONCLUSION/SIGNIFICANCE: The unique binding properties imply that COMPcc may be involved in signalling functions in which hydrophilic ligands are involved. The pentameric channel is a unique carrier for lipophilic compounds. This opens the exciting possibility that COMPcc could be developed as a targeted drug delivery system. The pentameric channel of COMPcc in complex with different fatty acids.,MacFarlane AA, Orriss G, Okun N, Meier M, Klonisch T, Khajehpour M, Stetefeld J PLoS One. 2012;7(11):e48130. doi: 10.1371/journal.pone.0048130. Epub 2012 Nov 2. PMID:23133613 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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