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Yorodumi- PDB-1n9u: Differences and Similarities in Solution Structures of Angiotensi... -
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-Basic information
Entry | Database: PDB / ID: 1n9u | ||||||
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Title | Differences and Similarities in Solution Structures of Angiotensin I & II: Implication for Structure-Function Relationship | ||||||
Components | Angiotensin I | ||||||
Keywords | SIGNALING PROTEIN / Angiotensin / Renin-Angiotensin System / Solid Phase Peptide Synthesis / NMR Solution Structure / Peptides | ||||||
Function / homology | Function and homology information regulation of blood volume by renin-angiotensin / response to muscle activity involved in regulation of muscle adaptation / type 2 angiotensin receptor binding / regulation of renal sodium excretion / maintenance of blood vessel diameter homeostasis by renin-angiotensin / negative regulation of neurotrophin TRK receptor signaling pathway / : / regulation of extracellular matrix assembly / regulation of renal output by angiotensin / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger ...regulation of blood volume by renin-angiotensin / response to muscle activity involved in regulation of muscle adaptation / type 2 angiotensin receptor binding / regulation of renal sodium excretion / maintenance of blood vessel diameter homeostasis by renin-angiotensin / negative regulation of neurotrophin TRK receptor signaling pathway / : / regulation of extracellular matrix assembly / regulation of renal output by angiotensin / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger / renin-angiotensin regulation of aldosterone production / renal system process / positive regulation of branching involved in ureteric bud morphogenesis / positive regulation of macrophage derived foam cell differentiation / positive regulation of extracellular matrix assembly / positive regulation of CoA-transferase activity / vasoconstriction / low-density lipoprotein particle remodeling / type 1 angiotensin receptor binding / positive regulation of extrinsic apoptotic signaling pathway / response to angiotensin / positive regulation of epidermal growth factor receptor signaling pathway / positive regulation of cardiac muscle hypertrophy / positive regulation of protein tyrosine kinase activity / positive regulation of gap junction assembly / regulation of cardiac conduction / regulation of vasoconstriction / blood vessel remodeling / Metabolism of Angiotensinogen to Angiotensins / positive regulation of epithelial to mesenchymal transition / nitric oxide-cGMP-mediated signaling / negative regulation of MAP kinase activity / positive regulation of protein metabolic process / positive regulation of endothelial cell migration / Peptide ligand-binding receptors / kidney development / positive regulation of cytokine production / angiotensin-activated signaling pathway / regulation of cell growth / growth factor activity / serine-type endopeptidase inhibitor activity / hormone activity / PPARA activates gene expression / regulation of blood pressure / positive regulation of miRNA transcription / positive regulation of inflammatory response / positive regulation of reactive oxygen species metabolic process / positive regulation of fibroblast proliferation / cell-cell signaling / positive regulation of NF-kappaB transcription factor activity / regulation of cell population proliferation / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (i) signalling events / G alpha (q) signalling events / collagen-containing extracellular matrix / regulation of apoptotic process / blood microparticle / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / G protein-coupled receptor signaling pathway / positive regulation of DNA-templated transcription / extracellular space / extracellular exosome / extracellular region Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Authors | Spyroulias, G.A. / Nikolakopoulou, P. / Tzakos, A. / Gerothanassis, I.P. / Magafa, V. / Manessi-Zoupa, E. / Cordopatis, P. | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 2003 Title: Comparison of the solution structures of angiotensin I & II. Implication for structure-function relationship. Authors: Spyroulias, G.A. / Nikolakopoulou, P. / Tzakos, A. / Gerothanassis, I.P. / Magafa, V. / Manessi-Zoupa, E. / Cordopatis, P. #1: Journal: J.Biol.Chem. / Year: 1994 Title: Role of the NH2-terminal domain of angiotensin II (ANG II) and [Sar1]angiotensin II on conformation and activity. NMR evidence for aromatic ring clustering and peptide backbone folding ...Title: Role of the NH2-terminal domain of angiotensin II (ANG II) and [Sar1]angiotensin II on conformation and activity. NMR evidence for aromatic ring clustering and peptide backbone folding compared with [des-1,2,3]angiotensin II Authors: Matsoukas, J.M. / Hondrelis, J. / Keramida, M. / Mavromoustakos, T. / Makriyannis, A. / Yamdagni, R. / Wu, Q. / Moore, G.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1n9u.cif.gz | 73.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1n9u.ent.gz | 52.5 KB | Display | PDB format |
PDBx/mmJSON format | 1n9u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1n9u_validation.pdf.gz | 340.8 KB | Display | wwPDB validaton report |
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Full document | 1n9u_full_validation.pdf.gz | 403.5 KB | Display | |
Data in XML | 1n9u_validation.xml.gz | 4.2 KB | Display | |
Data in CIF | 1n9u_validation.cif.gz | 6.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n9/1n9u ftp://data.pdbj.org/pub/pdb/validation_reports/n9/1n9u | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 1299.499 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: THE PEPTIDE WAS made through Solid phase synthesis using Fmoc chemistry. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN homo sapiens. References: UniProt: P01019 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. Models 1-20 are the family ensemble, while model 21 is the minimized average structure derived from that ensemble. |
-Sample preparation
Details | Contents: 2.5 mM; DMSO-d6 / Solvent system: DMSO-d6 |
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Sample conditions | Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DPX / Manufacturer: Bruker / Model: DPX / Field strength: 400 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 Details: This structure is based on a 225 NOE-derived distance constraints, 7 dihedral angle restraints, 1 distance restraint from hydrogen bond | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function for models 1-20, mean energy minimized for model 21 Conformers calculated total number: 300 / Conformers submitted total number: 21 |