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Yorodumi- PDB-1fvy: SOLUTION STRUCTURE OF THE OSTEOGENIC 1-31 FRAGMENT OF THE HUMAN P... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fvy | ||||||
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Title | SOLUTION STRUCTURE OF THE OSTEOGENIC 1-31 FRAGMENT OF THE HUMAN PARATHYROID HORMONE | ||||||
Components | PARATHYROID HORMONE | ||||||
Keywords | HORMONE/GROWTH FACTOR / HELIX-TURN-HELIX / PARATHYROID HORMONE / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | Function and homology information type 1 parathyroid hormone receptor binding / parathyroid hormone receptor binding / negative regulation of bone mineralization involved in bone maturation / positive regulation of osteoclast proliferation / negative regulation of apoptotic process in bone marrow cell / hormone-mediated apoptotic signaling pathway / response to parathyroid hormone / positive regulation of cell proliferation in bone marrow / magnesium ion homeostasis / positive regulation of signal transduction ...type 1 parathyroid hormone receptor binding / parathyroid hormone receptor binding / negative regulation of bone mineralization involved in bone maturation / positive regulation of osteoclast proliferation / negative regulation of apoptotic process in bone marrow cell / hormone-mediated apoptotic signaling pathway / response to parathyroid hormone / positive regulation of cell proliferation in bone marrow / magnesium ion homeostasis / positive regulation of signal transduction / macromolecule biosynthetic process / response to fibroblast growth factor / phosphate ion homeostasis / cAMP metabolic process / response to vitamin D / negative regulation of chondrocyte differentiation / Class B/2 (Secretin family receptors) / positive regulation of inositol phosphate biosynthetic process / peptide hormone receptor binding / bone mineralization / Rho protein signal transduction / : / positive regulation of glycogen biosynthetic process / positive regulation of bone mineralization / response to cadmium ion / homeostasis of number of cells within a tissue / bone resorption / skeletal system development / positive regulation of glucose import / response to lead ion / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / intracellular calcium ion homeostasis / cell-cell signaling / G alpha (s) signalling events / regulation of gene expression / response to ethanol / transcription by RNA polymerase II / receptor ligand activity / response to xenobiotic stimulus / G protein-coupled receptor signaling pathway / negative regulation of gene expression / positive regulation of gene expression / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Authors | Chen, Z. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Solution structure of the osteogenic 1-31 fragment of the human parathyroid hormone. Authors: Chen, Z. / Xu, P. / Barbier, J.R. / Willick, G. / Ni, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fvy.cif.gz | 209.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fvy.ent.gz | 172.1 KB | Display | PDB format |
PDBx/mmJSON format | 1fvy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fv/1fvy ftp://data.pdbj.org/pub/pdb/validation_reports/fv/1fvy | HTTPS FTP |
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-Related structure data
Similar structure data |
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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/peptide | Mass: 3726.354 Da / Num. of mol.: 1 / Fragment: RESIDUES 32-62 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P01270 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
-Sample preparation
Details | Contents: 1mM peptide; 25mM phosphate buffer; pH 6.8; 300mM NaCl; 90% H2O; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 6.8 / Temperature: 278 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |