+Open data
-Basic information
Entry | Database: PDB / ID: 1lre | ||||||
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Title | RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES | ||||||
Components | RECEPTOR-ASSOCIATED PROTEIN | ||||||
Keywords | CELL SURFACE PROTEIN / ALPHA2-MACROGLOBULIN RECEPTOR ASSOCIATED PROTEIN / LOW DENSITY LIPOPROTEIN RECEPTOR FAMILY ASSOCIATED PROTEIN / LDLR FAMILY ASSOCIATED PROTEIN / HELIX BUNDLE | ||||||
Function / homology | Function and homology information extracellular negative regulation of signal transduction / lipase binding / negative regulation of very-low-density lipoprotein particle clearance / regulation of receptor-mediated endocytosis / rough endoplasmic reticulum lumen / receptor antagonist activity / amyloid-beta clearance by transcytosis / negative regulation of amyloid-beta clearance / very-low-density lipoprotein particle receptor binding / positive regulation of amyloid-beta clearance ...extracellular negative regulation of signal transduction / lipase binding / negative regulation of very-low-density lipoprotein particle clearance / regulation of receptor-mediated endocytosis / rough endoplasmic reticulum lumen / receptor antagonist activity / amyloid-beta clearance by transcytosis / negative regulation of amyloid-beta clearance / very-low-density lipoprotein particle receptor binding / positive regulation of amyloid-beta clearance / cis-Golgi network / negative regulation of receptor internalization / low-density lipoprotein particle receptor binding / endoplasmic reticulum-Golgi intermediate compartment / endomembrane system / negative regulation of protein binding / endosome lumen / Golgi lumen / heparin binding / amyloid-beta binding / endosome / receptor ligand activity / signaling receptor binding / Golgi apparatus / cell surface / signal transduction / endoplasmic reticulum / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DG, MD | ||||||
Authors | Nielsen, P.R. / Poulsen, F.M. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1997 Title: The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. Authors: Nielsen, P.R. / Ellgaard, L. / Etzerodt, M. / Thogersen, H.C. / Poulsen, F.M. #1: Journal: To be Published Title: Alpha2-Macroglobulin Receptor Associated Proteins Consist of Three Domains with Similar Structural Motifs. The 1H, 15N, and 13C Chemical Shift Assignments and Secondary Structure of the ...Title: Alpha2-Macroglobulin Receptor Associated Proteins Consist of Three Domains with Similar Structural Motifs. The 1H, 15N, and 13C Chemical Shift Assignments and Secondary Structure of the Truncated N-Terminal Domain of Human RAP Authors: Nielsen, P.R. / Ellgaard, L. / Jensen, P.H. / Thoegersen, H.C. / Poulsen, F.M. #2: Journal: Eur.J.Biochem. / Year: 1997 Title: Dissection of the Domain Architecture of the Alpha2Macroglobulin-Receptor-Associated Protein Authors: Ellgaard, L. / Holtet, T.L. / Nielsen, P.R. / Etzerodt, M. / Gliemann, J. / Thogersen, H.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lre.cif.gz | 525 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lre.ent.gz | 441.2 KB | Display | PDB format |
PDBx/mmJSON format | 1lre.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lre_validation.pdf.gz | 345.3 KB | Display | wwPDB validaton report |
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Full document | 1lre_full_validation.pdf.gz | 517.1 KB | Display | |
Data in XML | 1lre_validation.xml.gz | 47.5 KB | Display | |
Data in CIF | 1lre_validation.cif.gz | 73.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lr/1lre ftp://data.pdbj.org/pub/pdb/validation_reports/lr/1lre | 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 | Mass: 9536.008 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN, DOMAIN 1, RESIDUES 17 - 97 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: BL21 / Plasmid: PT=7=H=6=UB / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: P30533 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Sample conditions | pH: 6.4 / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: DG, MD / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 20 |