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TitleStructure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 116, Issue 5, Page 1723-1732, Year 2019
Publish dateJan 29, 2019
AuthorsGabriel Birrane / Anne P Beigneux / Brian Dwyer / Bettina Strack-Logue / Kristian Kølby Kristensen / Omar L Francone / Loren G Fong / Haydyn D T Mertens / Clark Q Pan / Michael Ploug / Stephen G Young / Muthuraman Meiyappan /
PubMed AbstractLipoprotein lipase (LPL) is responsible for the intravascular processing of triglyceride-rich lipoproteins. The LPL within capillaries is bound to GPIHBP1, an endothelial cell protein with a three- ...Lipoprotein lipase (LPL) is responsible for the intravascular processing of triglyceride-rich lipoproteins. The LPL within capillaries is bound to GPIHBP1, an endothelial cell protein with a three-fingered LU domain and an N-terminal intrinsically disordered acidic domain. Loss-of-function mutations in or cause severe hypertriglyceridemia (chylomicronemia), but structures for LPL and GPIHBP1 have remained elusive. Inspired by our recent discovery that GPIHBP1's acidic domain preserves LPL structure and activity, we crystallized an LPL-GPIHBP1 complex and solved its structure. GPIHBP1's LU domain binds to LPL's C-terminal domain, largely by hydrophobic interactions. Analysis of electrostatic surfaces revealed that LPL contains a large basic patch spanning its N- and C-terminal domains. GPIHBP1's acidic domain was not defined in the electron density map but was positioned to interact with LPL's large basic patch, providing a likely explanation for how GPIHBP1 stabilizes LPL. The LPL-GPIHBP1 structure provides insights into mutations causing chylomicronemia.
External linksProc Natl Acad Sci U S A / PubMed:30559189 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.8 Å
Structure data

SASDDM9:
lipoprotein lipase–GPIHBP1 complex (Lipoprotein lipase, hLPL + Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1, GPIHBP1)
Method: SAXS/SANS

PDB-6e7k:
Structure of the lipoprotein lipase GPIHBP1 complex that mediates plasma triglyceride hydrolysis
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / hydrolase-cofactor complex / lipid degradation

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