Structural representation of the M1-fibrinogen interaction. M1 protein fragment (residues 132-263, ∼17 kDa) and 1 fibrinogen fragment D domain structure (∼86 kDa) in ribbon representation. PDB: 2XNX. M1 binds fibrinogen through the B1B2 domain (blue). Fibrinogen D fragment binds to M1 through β-chains (βArg169, βGlu173, βArg176) and γ-chains (γArg108, γTyr109, γSer116) depicted by the gray and black spheres, respectively. The E domain of fibrinogen, where thrombin cleaves fibrinopeptides A and B to initiate polymerization, is not illustrated. The location of holes “a” and D:D interfaces are highlighted (dark purple) to demonstrate spatial separation from M1 binding regions.
Figure 7.

Structural representation of the M1-fibrinogen interaction. M1 protein fragment (residues 132-263, ∼17 kDa) and 1 fibrinogen fragment D domain structure (∼86 kDa) in ribbon representation. PDB: 2XNX. M1 binds fibrinogen through the B1B2 domain (blue). Fibrinogen D fragment binds to M1 through β-chains (βArg169, βGlu173, βArg176) and γ-chains (γArg108, γTyr109, γSer116) depicted by the gray and black spheres, respectively. The E domain of fibrinogen, where thrombin cleaves fibrinopeptides A and B to initiate polymerization, is not illustrated. The location of holes “a” and D:D interfaces are highlighted (dark purple) to demonstrate spatial separation from M1 binding regions.

This Feature Is Available To Subscribers Only

or Create an Account

Close Modal
Close Modal