4xpj

Crystal structure of Nerve growth factor in complex with lysophosphatidylinositol

spinqualitylabelsall models 4xpj, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xpj is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.605Å Ligands: LPY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NGF_MOUSE Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades through those receptor tyrosine kinase to regulate neuronal proliferation, differentiation and survival. Publication Abstract from PubMed Nerve growth factor (NGF) is an important protein that is involved in a variety of physiological processes in cell survival, differentiation, proliferation and maintenance. The previously reported crystal structure of mouse NGF (mNGF) in complex with lysophosphatidylserine (LysoPS) showed that mNGF can bind LysoPS at its dimeric interface. To expand the understanding of the structural basis for specific lipid recognition by NGF, the crystal structure of mNGF complexed with lysophosphatidylinositol (13:0 LysoPI) was solved. Interestingly, in addition to Lys88, which interacts with the head glycerol group and the phosphate group of LysoPI, as seen in the mNGF-LysoPS structure, two additional residues, Tyr52 and Arg50, were found to assist in lipid binding by forming hydrogen bonds to the inositol moiety of the LysoPI molecule. The results suggest a specific recognition mechanism of inositol group-containing lipids by NGF, which may help in the design of bioactive compounds that can be delivered by NGF. The structure of nerve growth factor in complex with lysophosphatidylinositol.,Sun HL, Jiang T Acta Crystallogr F Struct Biol Commun. 2015 Jul;71(Pt 7):906-12. doi:, 10.1107/S2053230X15008870. Epub 2015 Jun 27. PMID:26144237 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nerve growth factor

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