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-Structure paper
| タイトル | Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis. |
|---|---|
| ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 116, Issue 5, Page 1723-1732, Year 2019 |
| 掲載日 | 2019年1月29日 |
著者 | Gabriel 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 要旨 | 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- ...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. |
リンク | Proc Natl Acad Sci U S A / PubMed:30559189 / PubMed Central |
| 手法 | SAS (X-ray synchrotron) / X線回折 |
| 解像度 | 2.8 Å |
| 構造データ | ![]() SASDDM9: ![]() PDB-6e7k: |
| 化合物 | ![]() ChemComp-CA: ![]() ChemComp-NAG: ![]() ChemComp-HOH: |
| 由来 |
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キーワード | HYDROLASE / hydrolase-cofactor complex / lipid degradation |
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