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Title: Characterization of the interaction of EEN and its domains with Ca2+ and proline rich domain
Keywords: Endophilin, EEN, PRD, SH3 domain, BAR domain
Issue Date: 12-Oct-2006
Citation: ZHANG YUNING (2006-10-12). Characterization of the interaction of EEN and its domains with Ca2+ and proline rich domain. ScholarBank@NUS Repository.
Abstract: EEN (Extra Eleven Nineteenth) is the human homology of Endophlin II and plays a crucial role in synaptic transmission and nervous system. EEN consists of 368 amino acids and exists as a dimer in vitro. According to secondary structure prediction and functions, EEN is divided into three domains: an alpha helical BAR (Bin/amphiphysin/Rvs) domain at C-terminus, a beta sheet SH3 (Src-homology-3) domain at N-terminus and a random coil domain between these two domains. To explore the possible role of this random coil domain, a polypeptide consisting of the SH3 domain and the random coil domain was designed and named as I?BAR domain. The EEN full length, BAR domain, SH3 domain and I?BAR domain were all cloned into pET-M, expressed in BL21(DE3) bacterial cell and purified with affinity and gel filtration columns. The interactions of Ca2+ and a peptide carrying the proline rich domain (PRD) with EEN and its three domains were investigated with NMR, ITC and other biochemical techniques. Our studies showed that Ca2+ has no influence on the structures of EEN, BAR domain and I?BAR domain in vitro. In addition, the random coil domain does not affect the bridging of SH3 domain to PRD in vitro. Therefore, the random coil domain or Ca2+ is not involved in interactions between the EEN SH3 domain and PRD.
Appears in Collections:Master's Theses (Open)

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