- PDB-1w0s: Solution structure of trimeric form of properdin by X-ray solutio... -
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Basic information
Entry
Database: PDB / ID: 1w0s
Title
Solution structure of trimeric form of properdin by X-ray solution scattering and analytical ultracentrifugation
Components
PROPERDIN
Keywords
GLYCOPROTEIN / X-RAY SCATTERING / ANALYTICAL ULTRACENTRIFUGATION / COMPLEMENT / THROMBOSPONDIN TYPE I REPEATS / CONSTRAINED MODELLING
Function / homology
Function and homology information
cytoplasmic side of Golgi membrane / positive regulation of opsonization / Defective B3GALTL causes PpS / O-glycosylation of TSR domain-containing proteins / Alternative complement activation / Activation of C3 and C5 / complement activation / complement activation, alternative pathway / Regulation of Complement cascade / specific granule lumen ...cytoplasmic side of Golgi membrane / positive regulation of opsonization / Defective B3GALTL causes PpS / O-glycosylation of TSR domain-containing proteins / Alternative complement activation / Activation of C3 and C5 / complement activation / complement activation, alternative pathway / Regulation of Complement cascade / specific granule lumen / positive regulation of immune response / tertiary granule lumen / defense response to bacterium / immune response / endoplasmic reticulum lumen / Neutrophil degranulation / extracellular space / extracellular region Similarity search - Function
Journal: J.Mol.Biol. / Year: 2004 Title: The Dimeric and Trimeric Solution Structures of the Multidomain Complement Protein Properdin by X-Ray Scattering, Analytical Ultracentrifugation and Constrained Modelling. Authors: Sun, Z. / Reid, K.B.M. / Perkins, S.J.
PROPERDIN / FACTOR P / Coordinate model: Cα atoms only
Mass: 48554.000 Da / Num. of mol.: 3 / Fragment: RESIDUES 28-469 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P27918
Compound details
POSITIVELY REGULATES THE ALTERNATE PATHWAY OF COMPLEMENT BY BINDING AND STABILIZING THE C3- AND C5- ...POSITIVELY REGULATES THE ALTERNATE PATHWAY OF COMPLEMENT BY BINDING AND STABILIZING THE C3- AND C5-CONVERTASE ENZYME COMPLEXES.
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Experimental details
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Experiment
Experiment
Method: SOLUTION SCATTERING
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Data collection
Soln scatter
Type
ID
Buffer name
Conc. range (mg/ml)
Data reduction software list
Detector type
Mean guiner radius (nm)
Mean guiner radius esd (nm)
Min mean cross sectional radii gyration (nm)
Min mean cross sectional radii gyration esd (nm)
Num. of time frames
Protein length
Source class
Source type
Temperature (K)
x-ray
1
140MMNACL, 10MMTRIS.HCL
0.25-1.00
MULTICCD
FRELONCCDCAMERA
10.34
0.36
1.51
0.2
10
30
Y
ESRFBEAMLINEID02
288
modelling
2
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Processing
Software
Name: INSIGHT / Version: II 98 / Classification: refinement
Refinement
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION
Refinement step
Cycle: LAST
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
1326
0
0
0
1326
Soln scatter model
Num. of conformers submitted: 1 / Software author list: MSI / Software list: INSIGHT II, SCTPL7, GNOM
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