| Type: | Domain | Name: | Fibrogen-binding domain 1 |
| Description: | This entry represents fibrinogen-binding domain 1. In proteins such as fibrinogen-binding adhesion SdrG and clumping factor A, there are two fibrinogen-binding domains with similar core beta-sandwich topologies, but with different modulations in their structure. This entry represents the first domain, while represents the second domain. Gram-positive pathogens, such as Staphylococci, Streptococci, and Enterococci, contain multiple cell wall-anchored proteins. Some of these proteins act as adhesins and mediate bacterial attachment to host tissues through lock-and-interactions with host ligands, such as fibrinogen, a glycoprotein found in blood plasma that plays a key role in haemostasis and coagulation. For pathogenic bacteria that do not invade host cells, extracellular matrix proteins are preferred targets for bacterial adhesion; adhesins mediating these interactions have been termed MSCRAMMs (microbial surface components recognizing adhesive matrix molecules). A common binding domain organisation found within MSCRAMMs suggests a common ancestry. Both fibrinogen-binding adhesion SdrG and clumping factor A are MSCRAMMs. Fibrinogen-binding adhesion SdrG is a cell wall-anchored adhesion found in the pathogen Mycobacterium farcinogenesthat binds to the B-beta chain of human fibrinogen [], while clumping factor A performs a similar function in Staphylococcus aureusby binding the gamma chain of fibrinogen []. | Short Name: | Fibrogen-bd_dom1 |
