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Open data
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Basic information
Entry | Database: PDB / ID: 3chn | ||||||
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Title | Solution structure of human secretory IgA1 | ||||||
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![]() | IMMUNE SYSTEM / Immunoglobulin A / Secretory immunoglobulin A / Mucosal immunity / neutron scattering / X-ray scattering / Chromophore / Glycoprotein / Immunoglobulin C region / Immunoglobulin domain / Membrane / Phosphoprotein / Secreted / Transmembrane | ||||||
Function / homology | ![]() polymeric immunoglobulin receptor activity / immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor / polymeric immunoglobulin binding / secretory dimeric IgA immunoglobulin complex / monomeric IgA immunoglobulin complex / secretory IgA immunoglobulin complex / Fc receptor signaling pathway / glomerular filtration / detection of chemical stimulus involved in sensory perception of bitter taste / IgA immunoglobulin complex ...polymeric immunoglobulin receptor activity / immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor / polymeric immunoglobulin binding / secretory dimeric IgA immunoglobulin complex / monomeric IgA immunoglobulin complex / secretory IgA immunoglobulin complex / Fc receptor signaling pathway / glomerular filtration / detection of chemical stimulus involved in sensory perception of bitter taste / IgA immunoglobulin complex / IgG immunoglobulin complex / azurophil granule membrane / receptor clustering / positive regulation of respiratory burst / Scavenging of heme from plasma / immunoglobulin complex, circulating / immunoglobulin receptor binding / complement activation, classical pathway / Cell surface interactions at the vascular wall / antigen binding / B cell receptor signaling pathway / epidermal growth factor receptor signaling pathway / antibacterial humoral response / adaptive immune response / receptor complex / blood microparticle / immune response / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Bonner, A. / Almogren, A. / Furtado, P.B. / Kerr, M.A. / Perkins, S.J. | ||||||
![]() | ![]() Title: Location of secretory component on the Fc edge of dimeric IgA1 reveals insight into the role of secretory IgA1 in mucosal immunity. Authors: Bonner, A. / Almogren, A. / Furtado, P.B. / Kerr, M.A. / Perkins, S.J. #1: ![]() Title: Implications of the near-planar solution structure of human myeloma dimeric IgA1 for mucosal immunity and IgA nephropathy Authors: Bonner, A. / Furtado, P.B. / Almogren, A. / Kerr, M.A. / Perkins, S.J. #2: ![]() Title: The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling Authors: Boehm, M.K. / Woof, J.M. / Kerr, M.A. / Perkins, S.J. #3: ![]() Title: Solution structure of human secretory component and implication for biological function Authors: Bonner, A. / Perrier, C. / Corthesy, B. / Perkins, S.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 798.3 KB | Display | ![]() |
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PDB format | ![]() | 661.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 415.9 KB | Display | ![]() |
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Full document | ![]() | 440.5 KB | Display | |
Data in XML | ![]() | 7.9 KB | Display | |
Data in CIF | ![]() | 310.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Number of models | 10 |
Details | The biological assembly of SIgA1 consists of four IgA1 heavy chains (A,B,C and D), four light chains (L, M, N and O), J chain (J) and secretory component (S). |
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Components
#1: Antibody | Mass: 23216.770 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Details: purified from human colostrum / Source: (natural) ![]() #2: Antibody | Mass: 51068.383 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Details: purified from human colostrum / Source: (natural) ![]() #3: Protein | | Mass: 11850.517 Da / Num. of mol.: 1 / Fragment: Ig-like V-type domain 4 / Source method: isolated from a natural source / Details: purified from human colostrum / Source: (natural) ![]() #4: Protein | | Mass: 64355.234 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: purified from human colostrum / Source: (natural) ![]() Sequence details | THE PART OF SEQUENCE BELONGS TO IGA VARIABLE HEAVY CHAIN. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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-Data collection
Diffraction |
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Detector |
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Radiation |
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Radiation wavelength |
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Soln scatter | Buffer name: 140 MM NACL 12.5 MM NAHPO4 0.5 MM EDTA 0.02% NA AZIDE / Data analysis software list: SCTPL7, GNOM / Protein length: 1 / Sample pH: 7.5 / Source class: Y / Temperature: 288 K
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Processing
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Refinement | Method to determine structure: CONSTRAINED MODELLING | |||||||||||||||||||||
Refinement step | Cycle: LAST
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Soln scatter model | Details: THE COORDINATES CONTAIN ONLY CA ATOMS. THE TEN BEST-FIT SOLUTION STRUCTURES HAVE BEEN DEPOSITED, WHERE MODEL 1 IS THE BEST-FIT SIGA1 SOLUTION STRUCTURE AND MODELS 2 TO 10 REPRESENT THE REST ...Details: THE COORDINATES CONTAIN ONLY CA ATOMS. THE TEN BEST-FIT SOLUTION STRUCTURES HAVE BEEN DEPOSITED, WHERE MODEL 1 IS THE BEST-FIT SIGA1 SOLUTION STRUCTURE AND MODELS 2 TO 10 REPRESENT THE REST OF THE FAMILY OF BEST-FIT STRUCTURES. Num. of conformers submitted: 10 / Representative conformer: 1 / Software list: INSIGHT II, SCTPL7, GNOM |