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Yorodumi- PDB-2bgr: Crystal structure of HIV-1 Tat derived nonapeptides Tat(1-9) boun... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2bgr | |||||||||
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Title | Crystal structure of HIV-1 Tat derived nonapeptides Tat(1-9) bound to the active site of Dipeptidyl peptidase IV (CD26) | |||||||||
Components |
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Keywords | HYDROLASE / HYDROLASE-COMPLEX / DPPIV / ALPHA/BETA-HYDROLASE FOLD / BETA-PROPELLER FOLD | |||||||||
Function / homology | Function and homology information viral gene expression / trans-activation response element binding / regulatory region RNA binding / protein serine/threonine phosphatase inhibitor activity / positive regulation of viral transcription / glucagon processing / modulation by virus of host chromatin organization / negative regulation of neutrophil chemotaxis / symbiont-mediated suppression of host translation initiation / Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) ...viral gene expression / trans-activation response element binding / regulatory region RNA binding / protein serine/threonine phosphatase inhibitor activity / positive regulation of viral transcription / glucagon processing / modulation by virus of host chromatin organization / negative regulation of neutrophil chemotaxis / symbiont-mediated suppression of host translation initiation / Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) / regulation of cell-cell adhesion mediated by integrin / negative regulation of extracellular matrix disassembly / psychomotor behavior / dipeptidyl-peptidase IV / intercellular canaliculus / host cell nucleolus / chemorepellent activity / actinin binding / dipeptidyl-peptidase activity / peptide hormone processing / negative regulation of peptidyl-threonine phosphorylation / locomotory exploration behavior / lamellipodium membrane / endocytic vesicle / endothelial cell migration / RNA-binding transcription regulator activity / behavioral fear response / aminopeptidase activity / T cell costimulation / T cell activation / serine-type peptidase activity / cyclin binding / positive regulation of transcription elongation by RNA polymerase II / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / virus receptor activity / lamellipodium / protease binding / host cell cytoplasm / receptor-mediated endocytosis of virus by host cell / membrane fusion / receptor-mediated virion attachment to host cell / response to hypoxia / cell adhesion / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont entry into host cell / membrane raft / apical plasma membrane / lysosomal membrane / protein domain specific binding / signaling receptor binding / serine-type endopeptidase activity / focal adhesion / DNA-templated transcription / positive regulation of cell population proliferation / cell surface / protein homodimerization activity / proteolysis / extracellular exosome / extracellular region / membrane / identical protein binding / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | HOMO SAPIENS (human) HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | |||||||||
Authors | Weihofen, W.A. / Liu, J. / Reutter, W. / Saenger, W. / Fan, H. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Crystal Structures of HIV-1 Tat-Derived Nonapeptides Tat-(1-9) and Trp2-Tat-(1-9) Bound to the Active Site of Dipeptidyl-Peptidase Iv (Cd26) Authors: Weihofen, W.A. / Liu, J. / Reutter, W. / Saenger, W. / Fan, H. | |||||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2bgr.cif.gz | 352.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2bgr.ent.gz | 284.3 KB | Display | PDB format |
PDBx/mmJSON format | 2bgr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bg/2bgr ftp://data.pdbj.org/pub/pdb/validation_reports/bg/2bgr | HTTPS FTP |
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-Related structure data
Related structure data | 2bgnC 1n1mS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1 / End auth comp-ID: SER / End label comp-ID: SER / Refine code: 6
NCS oper: (Code: given Matrix: (-0.946, 0.152, -0.287), Vector: |
-Components
-Protein / Protein/peptide / Non-polymers , 3 types, 1750 molecules ABYZ
#1: Protein | Mass: 85452.570 Da / Num. of mol.: 2 / Fragment: EXTRACELLULAR DOMAIN, RESIDUES 29-766 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Organ: KIDNEY / Plasmid: PFASTBACHTC / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / Strain (production host): SF9 CELLS / References: UniProt: P27487, dipeptidyl-peptidase IV #2: Protein/peptide | Mass: 1029.121 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 / References: UniProt: P12506 #8: Water | ChemComp-HOH / | |
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-Sugars , 5 types, 14 molecules
#3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||||
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#4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #5: Polysaccharide | Source method: isolated from a genetically manipulated source #6: Polysaccharide | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #7: Sugar | ChemComp-NAG / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.56 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 |
Detector | Type: ADSC CCD / Detector: CCD / Date: May 3, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 127470 / % possible obs: 92 % / Observed criterion σ(I): 2 / Redundancy: 4.3 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 19.8 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 4 % / Rmerge(I) obs: 0.37 / Mean I/σ(I) obs: 3.1 / % possible all: 87.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1N1M Resolution: 2→30 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.955 / SU B: 6.392 / SU ML: 0.095 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.147 / ESU R Free: 0.139 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 29 - 37 ARE DISORDERED AND WERE NOT MODELLED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.7 Å2
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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