Rebecca Martin/Sandbox1: Difference between revisions
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== IgA == | == Introduction to IgA == | ||
IgA1 | IgA is the most abundant antibody in the body 10064707 | ||
In fact, the body produces more IgA daily than than any other antibody 19079336 | |||
IgA is also unique, in that it exists in multiple oligomeric states. | |||
Two isotypes: IgA1 and IgA2 10064707 | |||
Unique- multi oligomeric forms 19079336 | |||
3 forms: monomer, dimer, (sometimes 3 or 4) secretory 10064707 | |||
Receptors: FcalphaR; pIgR, transferrin R (IgA1- recognizes O-glycosylation sites 15111057 ) | |||
IgA | |||
Participates in mucosal responses in the gut (IgA1~IgA2) and peripheral immune responses in the serum (90% monomeric IgA1) 10064707 | |||
Secretory IgA – primary immune defense 15111057 | |||
Neutralizes; immune exclusion commensals 19079336 | |||
Serum iga – second line of defense after m/o invade 15111057 | |||
{{STRUCTURE_1iga | PDB=1iga | SCENE= }} | {{STRUCTURE_1iga | PDB=1iga | SCENE= }} | ||
Revision as of 05:58, 23 April 2009
Introduction to IgAIntroduction to IgA
IgA is the most abundant antibody in the body 10064707 In fact, the body produces more IgA daily than than any other antibody 19079336 IgA is also unique, in that it exists in multiple oligomeric states. Two isotypes: IgA1 and IgA2 10064707 Unique- multi oligomeric forms 19079336 3 forms: monomer, dimer, (sometimes 3 or 4) secretory 10064707 Receptors: FcalphaR; pIgR, transferrin R (IgA1- recognizes O-glycosylation sites 15111057 ) IgA Participates in mucosal responses in the gut (IgA1~IgA2) and peripheral immune responses in the serum (90% monomeric IgA1) 10064707 Secretory IgA – primary immune defense 15111057 Neutralizes; immune exclusion commensals 19079336 Serum iga – second line of defense after m/o invade 15111057
StructureStructure
- Immunoglobulin Structure
Antibodies are composed of a heavy chain and a light chain.
Fab fragment
- Forms of IgA
Dimeric Structure
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- Secretory Component
IgA1 and IgA2IgA1 and IgA2
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Secretory ComponentSecretory Component
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Insights into FunctionInsights into Function
EvolutionEvolution
Implications in Science and MedicineImplications in Science and Medicine
Limitations of the Current StudiesLimitations of the Current Studies
- Because of the nature of the IgA molecule, crystalizing this structure was not possible. Therefore, many of these structures are based on models and not actual crystal structures. Because ...., the models were depositable in the PDB. I tried to include other crystallographic data when available, supporting the proposed models- as the authors did in the original papers.
Questions for the FutureQuestions for the Future
- Because of the limitating resolution of these models, many details concerning the binding residues and residue interactions are left unknown. Crystallographic structure will yield further insights into the structure of IgA, the interactions between IgA and other molecules, and ....
LinksLinks
IgAIgA
- Monomeric
- Fab and Fc Fragments
- Refined crystal structure of the galactan-binding immunoglobulin fab j539 at 1.95-angstroms resolution 2fbj
- Phosphocholine binding immunoglobulin fab mc/pc603. an x-ray diffraction study at 2.7 angstroms 1mcp
- Phosphocholine binding immunoglobulin fab mc/pc603. an x-ray diffraction study at 3.1 angstroms 2mcp
- Crystal structure of human FcaRI bound to IgA1-Fc 1ow0
- Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant 2imm and2imn
- Dimeric and Secretory
ReceptorsReceptors
- Crystal Structure of a Ligand-Binding Domain of the Human Polymeric Ig Receptor, pIgR 1XED
- Crystal structure of human FcaRI 10vz
- Crystal structure of a Staphylococcus aureus protein (SSL7) in complex with Fc of human IgA1 2qej
Other Isotypes (for comparison)Other Isotypes (for comparison)
- IgM: Solution structure of human Immunoglobulin M 2rcj
- IgG:
- IgD:
- IgE: