User:Thomas McNamara/Sandbox 1

From Proteopedia

Revision as of 22:19, 16 December 2018

Immunoglobulin G

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:

1) Neutralize/Immobilize the pathogen, preventing it from functioning; and/or 2) Bind to immune cell receptors that facilitate pathogen degradation.

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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References