Although 2r7e is plays a small role in one of many blood clotting factors, changes to its structure can have adverse effects, such as the onset of hemophilia More specifically, 2r7e is a polypeptide component of Coagulation Factor VIII. Coagulation Factor VIII plays an incredibly important role in thrombosis, and damage to its structure has been cited as a common cause of hemophilia a. Thus, changes to the 2r7e protein, such as the manipulation of ligand binding sites, could disrupt the function of the Coagulation Factor VIII protein complex, and, consequently, result in poor blood clotting performance.
2r7e is a cool protein.
Structural highlights
2r7e is a 2 chain structure. It has 5 associated ligands and is coded for by 2 different genes, F8 and F8C. 2r7e has both and secondary structure. Alterations in this structure can lead to improper location of ligands, leading to failed protein function. Also, most proteins including 2r7e, incorporate other macromolecules in order to create a stronger structure. In this case, 2r7e relies on to hold the structure together.
Ligands
2r7e has 5 ligands (, , BMA, MAN, NAG), which are binding sites for other proteins in Coagulation Factor VIII.
Function
2r7e is a protein that makes up part of Coagulation Factor VIII, which is a protein complex involved in blood clotting in humans. Coagulation Factor VIII works with calcium and phosholipids to Factor X to its activated form Xa.
Disease
Mutations in 2r7e can alter the structure of Coagulation Factor VIII, leading to hemophilia a.
Relevance
Yay!
References
h http://www.uniprot.org/uniprot/P00451
