Postgraduate Research Student,
The intrinsic pathway known as the contact pathway is involved in blood coagulation, inflammation and thrombosis. This pathway is initiated when FXII and High molecular weight kininogen (HMWK) bound… read more
The intrinsic pathway known as the contact pathway is involved in blood coagulation, inflammation and thrombosis. This pathway is initiated when FXII and High molecular weight kininogen (HMWK) bound to prekallikrein on the surface of cell receptor gC1qR. FXII and HMWK also bind to gC1qR in a zinc-dependent manner, triggering a downstream cascade that leads to release of inflammatory mediator bradykinin. Domain 5 of HMWK is showed to be responsible for the binding of HMWK and gC1qR. Previous works revealed one trimer of gC1qR is able to bind to 3 domain 5 ligands through different levels of affinities. Truncates of domain 5 were studied to narrow down the critical sequence of binding. Mutants of gC1qR were performed with deletion of the flexible loops to reduce the difficulty of crystallization.
My supervisor is Prof. Jonas Emsley. Below is the URL.
My current research aims to determine the structural information of interaction between gC1qR and HMWK. Mutants gC1qR and D5 truncates are also set up to improve the quality and probability of crystallization. The structural information is important to further understand how coagulation factors assemble on the cell surface with conformational change that initiate the coagulation pathway.
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