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Open data
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Basic information
Entry | Database: PDB / ID: 1lre | ||||||
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Title | RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES | ||||||
![]() | RECEPTOR-ASSOCIATED PROTEIN | ||||||
![]() | CELL SURFACE PROTEIN / ALPHA2-MACROGLOBULIN RECEPTOR ASSOCIATED PROTEIN / LOW DENSITY LIPOPROTEIN RECEPTOR FAMILY ASSOCIATED PROTEIN / LDLR FAMILY ASSOCIATED PROTEIN / HELIX BUNDLE | ||||||
Function / homology | ![]() 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 / receptor ligand activity / endosome / signaling receptor binding / Golgi apparatus / cell surface / signal transduction / endoplasmic reticulum / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DG, MD | ||||||
![]() | Nielsen, P.R. / Poulsen, F.M. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 525 KB | Display | ![]() |
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PDB format | ![]() | 441.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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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.) ![]() ![]() ![]() |
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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
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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 |