Title

The interaction between anastellin and beta-strands ABC, ABCD, and ABCDE from the 3rd type 3 domain of fibronectin

Presenter Information

Domnita-Valeria Rusnac

Presentation Type

Poster

Abstract

Every living organism contains thousands of proteins. It is known that there is tremendous variation in the forms and functions of proteins and almost all of them are essential for the proper functioning of the organism. Fibronectin is an extracellular matrix protein found in vertebrates including humans. It plays key roles in wound healing and embryonic development. Fibronectin forms thread like structures, termed fibrils, and the mechanism of this process is unknown. Anastellin, which is a fragment of fibronectin, interacts with fibronectin and triggers fibrogenesis in laboratory conditions. This model system has been developed to study the interactions between fibrils that could elucidate the mechanism of fibril formation. Fibronectin is composed of multiple structurally and functionally independent units: type I (FN1), type II (FN2) and type III (FN3) domains. Briknarova lab determined that the third type III domain of fibronectin (3FN3) and its truncated variants interact and form complexes with anastellin by using Gel Filtration. Some of these complexes adopt a well-defined three-dimensional structure, while others fluctuate among multiple conformations. In order to find out more about the interactions between anastellin and 3FN3 fragments, I cloned, expressed in E. coli, and purified by affinity chromatography different recombinant 3FN3 fragments (beta-strands ABC, ABCD, and ABCDE). The complexes with anastellin were analyzed by nuclear magnetic resonance (NMR) spectroscopy in order to obtain insight into the structure and dynamics of the complexes.

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Apr 13th, 11:00 AM Apr 13th, 12:00 PM

The interaction between anastellin and beta-strands ABC, ABCD, and ABCDE from the 3rd type 3 domain of fibronectin

UC Ballroom

Every living organism contains thousands of proteins. It is known that there is tremendous variation in the forms and functions of proteins and almost all of them are essential for the proper functioning of the organism. Fibronectin is an extracellular matrix protein found in vertebrates including humans. It plays key roles in wound healing and embryonic development. Fibronectin forms thread like structures, termed fibrils, and the mechanism of this process is unknown. Anastellin, which is a fragment of fibronectin, interacts with fibronectin and triggers fibrogenesis in laboratory conditions. This model system has been developed to study the interactions between fibrils that could elucidate the mechanism of fibril formation. Fibronectin is composed of multiple structurally and functionally independent units: type I (FN1), type II (FN2) and type III (FN3) domains. Briknarova lab determined that the third type III domain of fibronectin (3FN3) and its truncated variants interact and form complexes with anastellin by using Gel Filtration. Some of these complexes adopt a well-defined three-dimensional structure, while others fluctuate among multiple conformations. In order to find out more about the interactions between anastellin and 3FN3 fragments, I cloned, expressed in E. coli, and purified by affinity chromatography different recombinant 3FN3 fragments (beta-strands ABC, ABCD, and ABCDE). The complexes with anastellin were analyzed by nuclear magnetic resonance (NMR) spectroscopy in order to obtain insight into the structure and dynamics of the complexes.