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Yorodumi- PDB-1wbr: SOLUTION STRUCTURE OF THE HUMAN CD4 (403-419) RECEPTOR PEPTIDE, N... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wbr | ||||||
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Title | SOLUTION STRUCTURE OF THE HUMAN CD4 (403-419) RECEPTOR PEPTIDE, NMR, 32 STRUCTURES | ||||||
Components | CD4 RECEPTOR | ||||||
Keywords | IMMUNOGLOBULIN FOLD / CD4(403-419) RECEPTOR PEPTIDE / HIV / VPU | ||||||
Function / homology | Function and homology information helper T cell enhancement of adaptive immune response / interleukin-16 binding / interleukin-16 receptor activity / maintenance of protein location in cell / T cell selection / MHC class II protein binding / cellular response to granulocyte macrophage colony-stimulating factor stimulus / interleukin-15-mediated signaling pathway / positive regulation of monocyte differentiation / Nef Mediated CD4 Down-regulation ...helper T cell enhancement of adaptive immune response / interleukin-16 binding / interleukin-16 receptor activity / maintenance of protein location in cell / T cell selection / MHC class II protein binding / cellular response to granulocyte macrophage colony-stimulating factor stimulus / interleukin-15-mediated signaling pathway / positive regulation of monocyte differentiation / Nef Mediated CD4 Down-regulation / Alpha-defensins / positive regulation of kinase activity / regulation of T cell activation / T cell receptor complex / extracellular matrix structural constituent / Other interleukin signaling / enzyme-linked receptor protein signaling pathway / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / regulation of calcium ion transport / macrophage differentiation / Generation of second messenger molecules / T cell differentiation / PD-1 signaling / positive regulation of protein kinase activity / Binding and entry of HIV virion / coreceptor activity / positive regulation of calcium-mediated signaling / cell surface receptor protein tyrosine kinase signaling pathway / T cell activation / positive regulation of interleukin-2 production / protein tyrosine kinase binding / Vpu mediated degradation of CD4 / calcium-mediated signaling / clathrin-coated endocytic vesicle membrane / transmembrane signaling receptor activity / positive regulation of peptidyl-tyrosine phosphorylation / Downstream TCR signaling / Cargo recognition for clathrin-mediated endocytosis / positive regulation of T cell activation / MHC class II protein complex binding / Clathrin-mediated endocytosis / virus receptor activity / signaling receptor activity / positive regulation of canonical NF-kappaB signal transduction / defense response to Gram-negative bacterium / adaptive immune response / positive regulation of MAPK cascade / positive regulation of viral entry into host cell / positive regulation of ERK1 and ERK2 cascade / cell surface receptor signaling pathway / early endosome / cell adhesion / positive regulation of protein phosphorylation / immune response / membrane raft / endoplasmic reticulum lumen / external side of plasma membrane / lipid binding / endoplasmic reticulum membrane / protein kinase binding / positive regulation of DNA-templated transcription / enzyme binding / signal transduction / protein homodimerization activity / zinc ion binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
Authors | Willbold, D. / Roesch, P. | ||||||
Citation | Journal: J.Biomed.Sci. / Year: 1996 Title: Solution Structure of the Human CD4 (403-419) Receptor Peptide. Authors: Willbold, D. / Rosch, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wbr.cif.gz | 174 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wbr.ent.gz | 136.3 KB | Display | PDB format |
PDBx/mmJSON format | 1wbr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1wbr_validation.pdf.gz | 342.9 KB | Display | wwPDB validaton report |
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Full document | 1wbr_full_validation.pdf.gz | 534.4 KB | Display | |
Data in XML | 1wbr_validation.xml.gz | 11.4 KB | Display | |
Data in CIF | 1wbr_validation.cif.gz | 19.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wb/1wbr ftp://data.pdbj.org/pub/pdb/validation_reports/wb/1wbr | HTTPS FTP |
-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: 2075.479 Da / Num. of mol.: 1 / Fragment: 403 - 419 / Mutation: N-TERMINUS IS ACETYLATED, C-TERMINUS IS AMIDATED Source method: isolated from a genetically manipulated source Details: CHEMICALLY SYNTHESIZED / Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P01730 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: NOESY (150 MS MIXING TIME) |
-Sample preparation
Sample conditions | pH: 7.0 / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX600 / Manufacturer: Bruker / Model: AMX600 / Field strength: 600 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: ENERGY, AGREEMENT WITH EXPERIMENTAL DATA Conformers calculated total number: 50 / Conformers submitted total number: 32 |