Sandbox caroldavila
From Proteopedia
=[Image:Opening 1igt.png|450px|left|thumb| Intact Immunoglobulin, 1igt]]
| |||||||||
| Structura IGG B12 uman: o monstra pentru un potential vaccin HIV, 1hzh | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Antibodies, also known as Immunoglobulins (Ig) are gamma globulin proteins, primarily found in the blood of vertebrates. These glycoproteins serve as a critical component of the immune system when the host fails to activate alternative compliment pathways or phagocytic cells in response to invading microorganisms or other antigens. The incredible specificity with which immunoglobulins bind to an antigen is based upon structural complementarity between the antigen and antibody and . It is this specificity that has made a critical component in laboratory and medical research.
Contents |
Structure of the Immunoglobulin
Template:STRUCTURE 1igt The basic functional unit of an antibody is an immunoglobulin monomer, but antibodies secreted from plasma cells are typically dimeric with occasional higher order structures. Typical secreted antibodies have a basic four-peptide structure of two identical and two identical joined together by interchain , forming a “Y” shaped molecule. The disulfide bonds are positioned within a flexible region called the , which seperates the lobes of the antibody from one another and provides ample flexibility to bind antigens effectively. [1] Each domain (2 heavy and 2 light) contain between 70-110 amino acids and are classified into different categories according to size and function. [2] Both domains, heavy and light, contain variable and constant regions that are crucial to antibody function. [3]
