+Open data
-Basic information
Entry | Database: PDB / ID: 2jod | ||||||
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Title | Pac1-Rshort N-terminal EC domain Pacap(6-38) complex | ||||||
Components |
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Keywords | SIGNALING PROTEIN / protein-peptide complex | ||||||
Function / homology | Function and homology information negative regulation of response to reactive oxygen species / development of primary female sexual characteristics / pituitary adenylate cyclase activating polypeptide activity / vasoactive intestinal polypeptide receptor activity / positive regulation of growth hormone secretion / positive regulation of chemokine (C-C motif) ligand 5 production / positive regulation of cAMP-mediated signaling / NGF-independant TRKA activation / regulation of G protein-coupled receptor signaling pathway / neuropeptide hormone activity ...negative regulation of response to reactive oxygen species / development of primary female sexual characteristics / pituitary adenylate cyclase activating polypeptide activity / vasoactive intestinal polypeptide receptor activity / positive regulation of growth hormone secretion / positive regulation of chemokine (C-C motif) ligand 5 production / positive regulation of cAMP-mediated signaling / NGF-independant TRKA activation / regulation of G protein-coupled receptor signaling pathway / neuropeptide hormone activity / G protein-coupled peptide receptor activity / neuropeptide binding / positive regulation of small GTPase mediated signal transduction / insulin secretion / positive regulation of inositol phosphate biosynthetic process / peptide hormone receptor binding / positive regulation of calcium ion transport into cytosol / peptide hormone binding / adenylate cyclase binding / negative regulation of cell cycle / neuropeptide signaling pathway / bicellular tight junction / positive regulation of protein kinase activity / multicellular organismal response to stress / activation of adenylate cyclase activity / cAMP-mediated signaling / positive regulation of GTPase activity / caveola / female pregnancy / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / small GTPase binding / Glucagon-type ligand receptors / regulation of protein localization / neuron projection development / response to estradiol / cell-cell signaling / signaling receptor activity / positive regulation of cold-induced thermogenesis / positive regulation of cytosolic calcium ion concentration / G alpha (s) signalling events / spermatogenesis / perikaryon / response to ethanol / receptor complex / positive regulation of ERK1 and ERK2 cascade / endosome / cell differentiation / cell surface receptor signaling pathway / neuron projection / response to xenobiotic stimulus / intracellular membrane-bounded organelle / signaling receptor binding / cell surface / positive regulation of transcription by RNA polymerase II / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | Olejniczak, E.T. / Sun, C. / Song, D. / Davis-Taber, R.A. / Barrett, L.W. / Scott, V.E. / Richardson, P.L. / Pereda-lopez, A. / Uchic, M.E. / Solomon, L.R. ...Olejniczak, E.T. / Sun, C. / Song, D. / Davis-Taber, R.A. / Barrett, L.W. / Scott, V.E. / Richardson, P.L. / Pereda-lopez, A. / Uchic, M.E. / Solomon, L.R. / Lake, M.R. / Walter, K.A. / Hajduk, P.J. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2007 Title: Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS. Authors: Sun, C. / Song, D. / Davis-Taber, R.A. / Barrett, L.W. / Scott, V.E. / Richardson, P.L. / Pereda-Lopez, A. / Uchic, M.E. / Solomon, L.R. / Lake, M.R. / Walter, K.A. / Hajduk, P.J. / Olejniczak, E.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jod.cif.gz | 59.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jod.ent.gz | 43.8 KB | Display | PDB format |
PDBx/mmJSON format | 2jod.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2jod_validation.pdf.gz | 396.1 KB | Display | wwPDB validaton report |
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Full document | 2jod_full_validation.pdf.gz | 399.8 KB | Display | |
Data in XML | 2jod_validation.xml.gz | 5.9 KB | Display | |
Data in CIF | 2jod_validation.cif.gz | 7.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jo/2jod ftp://data.pdbj.org/pub/pdb/validation_reports/jo/2jod | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11989.428 Da / Num. of mol.: 1 / Fragment: residues 22-143 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ADCYAP1R1 / Production host: Escherichia coli (E. coli) / References: UniProt: P41586 |
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#2: Protein/peptide | Mass: 4036.815 Da / Num. of mol.: 1 / Fragment: sequence database residues, 137-169 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ADCYAP1 / Production host: Escherichia coli (E. coli) / References: UniProt: P18509 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 3D 1H-13C NOESY |
-Sample preparation
Details | Contents: 0.5 mM [U-100% 13C; U-100% 15N] pac1-R N-terminal EC domain, 0.5 mM PACAP (6-38), 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100 / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software | Name: CNS / Developer: Brunger, Adams, Clore, Gros, Nilges and Read / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR representative | Selection criteria: minimized average structure |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 300 / Conformers submitted total number: 1 |