User:Thomas McNamara/Sandbox 1
From Proteopedia
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Immunoglobulin G proteins, more commonly referred to as antibodies, make up a large family of secreted proteins that are potent regulators of the immune system. Furthermore, Immunoglobulin G proteins are the most common type of antibodies present in the serum, and utilize their two identical, but very unique, binding sites to recognize pathogens. It is these binding sites that differ in amino acid sequence between each Immunoglobulin G protein in a particular organism, giving each antibody a different binding target -- ultimately giving the immune system a large class of weapons that can bind to and recognize almost any foreign pathogen. | Immunoglobulin G proteins, more commonly referred to as antibodies, make up a large family of secreted proteins that are potent regulators of the immune system. Furthermore, Immunoglobulin G proteins are the most common type of antibodies present in the serum, and utilize their two identical, but very unique, binding sites to recognize pathogens. It is these binding sites that differ in amino acid sequence between each Immunoglobulin G protein in a particular organism, giving each antibody a different binding target -- ultimately giving the immune system a large class of weapons that can bind to and recognize almost any foreign pathogen. | ||
| - | This is a default text for your page '''Thomas McNamara/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs./Users/Tom/Desktop/AntibodyStrucMovie.mov | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function == | == Function == | ||
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| + | When a foreign pathogen invades a host organism, it is constantly coming into contact with circulating B-cells. Eventually, one particular B-cell will contain a membrane protein that recognizes and binds to a very specific region on the pathogen, called an epitope. This B-cell will then begin secreting identical Immunoglobulin G proteins whose binding sites recognize only the particular epitope. The secreted antibodies will then circulate throughout the host organism, searching for and binding to any other identical pathogens that display the same epitope. Once bound to the pathogen, the Immunoglobulin G protein can either: | ||
== Disease == | == Disease == | ||
Revision as of 22:15, 16 December 2018
Contents |
Immunoglobulin G
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Immunoglobulin G proteins, more commonly referred to as antibodies, make up a large family of secreted proteins that are potent regulators of the immune system. Furthermore, Immunoglobulin G proteins are the most common type of antibodies present in the serum, and utilize their two identical, but very unique, binding sites to recognize pathogens. It is these binding sites that differ in amino acid sequence between each Immunoglobulin G protein in a particular organism, giving each antibody a different binding target -- ultimately giving the immune system a large class of weapons that can bind to and recognize almost any foreign pathogen.
Function
When a foreign pathogen invades a host organism, it is constantly coming into contact with circulating B-cells. Eventually, one particular B-cell will contain a membrane protein that recognizes and binds to a very specific region on the pathogen, called an epitope. This B-cell will then begin secreting identical Immunoglobulin G proteins whose binding sites recognize only the particular epitope. The secreted antibodies will then circulate throughout the host organism, searching for and binding to any other identical pathogens that display the same epitope. Once bound to the pathogen, the Immunoglobulin G protein can either:
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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