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Yorodumi- SASDDM9: lipoprotein lipase–GPIHBP1 complex (Lipoprotein lipase, hLPL + Gl... -
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-Basic information
Entry | Database: SASBDB / ID: SASDDM9 |
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Sample | lipoprotein lipase–GPIHBP1 complex
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Function / homology | Function and homology information lipoprotein lipase / lipoprotein lipase activity / positive regulation of sequestering of triglyceride / low-density lipoprotein particle mediated signaling / chylomicron remodeling / positive regulation of cholesterol storage / phospholipase A1 / phosphatidylserine 1-acylhydrolase activity / 1-acyl-2-lysophosphatidylserine acylhydrolase activity / phospholipase A1 activity ...lipoprotein lipase / lipoprotein lipase activity / positive regulation of sequestering of triglyceride / low-density lipoprotein particle mediated signaling / chylomicron remodeling / positive regulation of cholesterol storage / phospholipase A1 / phosphatidylserine 1-acylhydrolase activity / 1-acyl-2-lysophosphatidylserine acylhydrolase activity / phospholipase A1 activity / phospholipase activity / triglyceride catabolic process / Assembly of active LPL and LIPC lipase complexes / very-low-density lipoprotein particle remodeling / positive regulation of macrophage derived foam cell differentiation / Chylomicron remodeling / positive regulation of lipid storage / chylomicron / cellular response to nutrient / very-low-density lipoprotein particle / triglyceride lipase activity / positive regulation of chemokine (C-X-C motif) ligand 2 production / heparan sulfate proteoglycan binding / triglyceride homeostasis / cellular response to fatty acid / triglyceride metabolic process / lipoprotein particle binding / apolipoprotein binding / catalytic complex / positive regulation of fat cell differentiation / phospholipid metabolic process / response to glucose / protein-membrane adaptor activity / Retinoid metabolism and transport / positive regulation of chemokine production / positive regulation of adipose tissue development / fatty acid metabolic process / positive regulation of interleukin-1 beta production / cholesterol homeostasis / response to bacterium / fatty acid biosynthetic process / Transcriptional regulation of white adipocyte differentiation / positive regulation of inflammatory response / positive regulation of interleukin-6 production / positive regulation of tumor necrosis factor production / heparin binding / signaling receptor binding / calcium ion binding / cell surface / protein homodimerization activity / extracellular space / extracellular region / plasma membrane Similarity search - Function |
Biological species | Homo sapiens (human) |
Citation | Journal: Proc Natl Acad Sci U S A / Year: 2019 Title: Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis. Authors: 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 / ...Authors: 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 / Abstract: 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. |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDDM9 |
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-Related structure data
-External links
Related items in Molecule of the Month |
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-Models
Model #2159 | Type: dummy / Software: (2.8.1) / Radius of dummy atoms: 2.20 A / Symmetry: P2 / Chi-square value: 1.067 / P-value: 0.382446 Search similar-shape structures of this assembly by Omokage search (details) |
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-Sample
Sample | Name: lipoprotein lipase–GPIHBP1 complex / Specimen concentration: 0.72 mg/ml / Entity id: 1184 / 1185 |
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Buffer | Name: 10 mM BisTris, 150 mM NaCl, 4 mM CaCl2, 10% glycerol / pH: 7.4 |
Entity #1184 | Name: hLPL / Type: protein / Description: Lipoprotein lipase / Formula weight: 50.323 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: P06858 Sequence: DQRRDFIDIE SKFALRTPED TAEDTCHLIP GVAESVATCH FNHSSKTFMV IHGWTVTGMY ESWVPKLVAA LYKREPDSNV IVVDWLSRAQ EHYPVSAGYT KLVGQDVARF INWMEEEFNY PLDNVHLLGY SLGAHAAGIA GSLTNKKVNR ITGLDPAGPN FEYAEAPSRL ...Sequence: DQRRDFIDIE SKFALRTPED TAEDTCHLIP GVAESVATCH FNHSSKTFMV IHGWTVTGMY ESWVPKLVAA LYKREPDSNV IVVDWLSRAQ EHYPVSAGYT KLVGQDVARF INWMEEEFNY PLDNVHLLGY SLGAHAAGIA GSLTNKKVNR ITGLDPAGPN FEYAEAPSRL SPDDADFVDV LHTFTRGSPG RSIGIQKPVG HVDIYPNGGT FQPGCNIGEA IRVIAERGLG DVDQLVKCSH ERSIHLFIDS LLNEENPSKA YRCSSKEAFE KGLCLSCRKN RCNNLGYEIN KVRAKRSSKM YLKTRSQMPY KVFHYQVKIH FSGTESETHT NQAFEISLYG TVAESENIPF TLPEVSTNKT YSFLIYTEVD IGELLMLKLK WKSDSYFSWS DWWSSPGFAI QKIRVKAGET QKKVIFCSRE KVSHLQKGKA PAVFVKCHDK SLNKKSG |
Entity #1185 | Name: GPIHBP1 / Type: protein Description: Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 Formula weight: 14.713 / Num. of mol.: 2 / Source: Homo sapiens Sequence: QTQQEEEEED EDHGPDDYDE EDEDEVEEEE TNRLPGGRSR VLLRCYTCKS LPRDERCNLT QNCSHGQTCT TLIAHGNTES GLLTTHSTWC TDSCQPITKT VEGTQVTMTC CQSSLCNVPP WQSSRVQDPT G |
-Experimental information
Beam | Instrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3.1 mm | ||||||||||||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 2M | ||||||||||||||||||||||||||||||||||||||||||
Scan | Title: lipoprotein lipase–GPIHBP1 complex / Measurement date: Dec 2, 2017 / Storage temperature: 25 °C / Cell temperature: 25 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 787 /
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Result | Type of curve: single_conc
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