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Yorodumi- PDB-6m6f: Solution structure of disulfide bond mutaion of the core domain o... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6m6f | |||||||||
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Title | Solution structure of disulfide bond mutaion of the core domain of Fibroblast growth factor 21 (FGF21) | |||||||||
Components | Fibroblast growth factor 21 | |||||||||
Keywords | HORMONE / Disulfide bond mutaion / beta-trefoil conformation / beta-klotho binding / Metabolic regulator | |||||||||
Function / homology | Function and homology information positive regulation of triglyceride catabolic process / Cellular hexose transport / response to methionine / Assembly of active LPL and LIPC lipase complexes / positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway / regulation of low-density lipoprotein particle clearance / fibroblast growth factor receptor binding / endothelial cell apoptotic process / positive regulation of low-density lipoprotein receptor activity / cellular response to glucagon stimulus ...positive regulation of triglyceride catabolic process / Cellular hexose transport / response to methionine / Assembly of active LPL and LIPC lipase complexes / positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway / regulation of low-density lipoprotein particle clearance / fibroblast growth factor receptor binding / endothelial cell apoptotic process / positive regulation of low-density lipoprotein receptor activity / cellular response to glucagon stimulus / cellular response to low-density lipoprotein particle stimulus / fibroblast growth factor receptor signaling pathway / negative regulation of endothelial cell apoptotic process / endoplasmic reticulum unfolded protein response / regulation of cell migration / response to nutrient levels / response to activity / cellular response to glucose stimulus / positive regulation of glucose import / animal organ morphogenesis / growth factor activity / cellular response to xenobiotic stimulus / cell-cell signaling / positive regulation of cold-induced thermogenesis / cell differentiation / positive regulation of ERK1 and ERK2 cascade / positive regulation of protein phosphorylation / positive regulation of cell population proliferation / positive regulation of gene expression / signal transduction / extracellular space / extracellular region / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Authors | Zhu, L. / Zhao, H. / Wang, J. | |||||||||
Funding support | China, 2items
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Citation | Journal: Embo Rep. / Year: 2021 Title: Dynamic folding modulation generates FGF21 variant against diabetes. Authors: Zhu, L. / Zhao, H. / Liu, J. / Cai, H. / Wu, B. / Liu, Z. / Zhou, S. / Liu, Q. / Li, X. / Bao, B. / Liu, J. / Dai, H. / Wang, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6m6f.cif.gz | 388.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6m6f.ent.gz | 325.3 KB | Display | PDB format |
PDBx/mmJSON format | 6m6f.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m6/6m6f ftp://data.pdbj.org/pub/pdb/validation_reports/m6/6m6f | HTTPS FTP |
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-Related structure data
Related structure data | 6m6eC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14103.977 Da / Num. of mol.: 1 Mutation: D23S, D24G, A25P, Q26H, Q28L, T29S, E30S, A31C, G43C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FGF21 / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: Q9NSA1 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 160 mM / Label: condition_1 / pH: 7.0 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 5 | ||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 10 |