Auxílio à Eventos para Alunos Matriculados
O envio dos pedidos será via e-mail (email@example.com)
- Café com Química
Data: 25 de abril, quarta-feira
Horário: 17h00 - Sala: IQ-06
"Refugiados do século XXI"
GT Cátedra Sérgio Vieira de Mello para Refugiados - UNICAMP
Resumo: O Grupo de Trabalho Cátedra dos Refugiados da UNICAMP - composto por docentes de diferentes unidades
e em parceria com a Prefeitura de Campinas e Agemcamp - apresentará as preocupações teóricas que envolvem o próprio
conceito de refugiado no mundo contemporâneo, incluindo os solicitantes de refúgio. Será discutido também o panorama atual
da migração refugiada no Brasil e os fluxos migratórios recentes vindos da Síria, República Democrática do Congo, Venezuela,
dentre outros, que também chegam a Campinas. Nesse contexto, serão discutidas as especificidades de diferentes campos
disciplinares para tratar da questão do refúgio (língua, saúde, educação, cultura, direitos).
Na oportunidade serão apresentadas as ações da Cátedra na Unicamp, destacando a Exposição Refugiados na Biblioteca Central.
Date: April 26 (Thursday), at 4 p.m.
Place: Room IQ-05.
"Fragment based drug development: Rational targeting of the Signal Recognition Particle Receptor".
Dr. Sandro F. Ataide, Lecturer in Structural Biology - SoLES | Faculty of Science - The University of Sydney.
Responsible: Prof. Ljubica Tasic, Ph.D.
Abstract: The signal recognition particle (SRP) is an essential ribonucleoprotein complex responsible for the co-translational delivery of membrane and secretory proteins to the plasma membrane in bacteria and to the endoplasmic reticulum in eukaryotes. In Eubacteria, SRP consists of one protein (Ffh), and a 4.5S RNA. The SRP cycle involves recognition of the signal peptide (SP) on the translating ribosome ( RNC) by the SRP followed by complex formation with SRP Receptor (SR) upon GTP binding and finally the delivery of the RNC to the translocon and GTP hydrolysis. The process is controlled by a series of coordinated conformational changes in each step that leads to the GTPase activity by SRP and SR.
An interesting point identified in previous crystal structures of the bacterial SRP complex with SR (FtsY) indicated new and specific interactions of SR with SRP RNA. Truncations or mutations on any of the bacterial components of the SRP system have proven to be either lethal or severely impact cell viability, indicating that disruption of this system could be a suitable target for drug discovery.
In order to investigate how cofactors such as GTP modulate FtsY structure and its interactions with RNA, we have analyzed the binding of FtsY to GTP analogues, such as GMPPNP and GCPPNP as well as to GDP and 4.5S RNA using Nuclear Magnetic Resonance (NMR) spectroscopy and crystallography. We have crystallized a longer construct of E. coli FtsY than the ones published before (termed NG+1 which comprises the NG domain with an extra Phe at the N-terminus that stabilizes the first helix in the structure) in an apo form that diffracts to much higher resolution at 1.35 Å. We have tested soaking conditi on for GTP analogues and GDP and have solved structures of these bound to NG+1 at 1.6 Å. We now have a robust methodology that yields crystals that diffract to high resolution enabling us to use it to characterize potential drugs that interact with FtsY.