Crystal structures of chloro(meso-tetraphenylporphyrinato)germanium(IV), Ge(tpp)Cl2, and dihydroxo(meso-tetraphenylporphyrinato)germanium(IV), Ge(tpp)(OH)2, and two-stage hydrolysis of its homologue dimethoxo(meso-tetraphenylporphyrinato)germanium(IV), Ge(tpp)(OMe)2

The 2,5-bis(2-arylvinyl)-1,4-benzoquinones 1a-1e are formed from hydrolysis of their corresponding ketals 5 which are generated by anodic oxidation of the corresponding 1,4-dimethoxybenzene derivatives 4. The crystal structures of the quinone compounds 1a, 1d and 1e have been determined by X-ray analyses. The bond lengths of the quinone system are influenced by polar resonance structures. An α-type packing mode is observed for the three crystal structures of compounds 1. The vinylic double bonds have short intermolecular distances (1a: 4.417(5), 1d: 3.653(2), 1e: 4.224(5) Å). Only the crystals of 1d with the shortest contacts are photoreactive

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Copper(II)-assisted hydrolysis of 2,4,6-tris(2-pyridyl)-1,3,5-triazine. Part 1. Crystal structures of [bis(2-pyridylcarbonyl)amido](2-pyridylformamide)-copper(II) perchlorate monohydrate and [bis(2-pyridylcarbonyl)amido]-copper(II) perchlorate

Journal of the Chemical Society Dalton Transactions ◽

10.1039/dt9880002033 ◽

1988 ◽

pp. 2033-2039 ◽

Cited By ~ 38

Author(s):

Andrés Cantarero ◽

Josep M. Amigó ◽

Juan Faus ◽

Miguel Julve ◽

Tony Debaerdemaeker

Keyword(s):

Crystal Structures ◽

Hydrolysis Of

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Structure of lipoprotein lipase in complex with GPIHBP1

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1820171116 ◽

2019 ◽

Vol 116 (21) ◽

pp. 10360-10365 ◽

Cited By ~ 13

Author(s):

Rishi Arora ◽

Amitabh V. Nimonkar ◽

Daniel Baird ◽

Chunhua Wang ◽

Chun-Hao Chiu ◽

...

Keyword(s):

Crystal Structures ◽

Lipoprotein Lipase ◽

Structural Information ◽

Density Lipoprotein ◽

Lipid Binding ◽

Structural Basis ◽

Maturation Factor ◽

Lipase Maturation Factor 1 ◽

Hydrolysis Of

Lipoprotein lipase (LPL) plays a central role in triglyceride (TG) metabolism. By catalyzing the hydrolysis of TGs present in TG-rich lipoproteins (TRLs), LPL facilitates TG utilization and regulates circulating TG and TRL concentrations. Until very recently, structural information for LPL was limited to homology models, presumably due to the propensity of LPL to unfold and aggregate. By coexpressing LPL with a soluble variant of its accessory protein glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 (GPIHBP1) and with its chaperone protein lipase maturation factor 1 (LMF1), we obtained a stable and homogenous LPL/GPIHBP1 complex that was suitable for structure determination. We report here X-ray crystal structures of human LPL in complex with human GPIHBP1 at 2.5–3.0 Å resolution, including a structure with a novel inhibitor bound to LPL. Binding of the inhibitor resulted in ordering of the LPL lid and lipid-binding regions and thus enabled determination of the first crystal structure of LPL that includes these important regions of the protein. It was assumed for many years that LPL was only active as a homodimer. The structures and additional biochemical data reported here are consistent with a new report that LPL, in complex with GPIHBP1, can be active as a monomeric 1:1 complex. The crystal structures illuminate the structural basis for LPL-mediated TRL lipolysis as well as LPL stabilization and transport by GPIHBP1.

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