Structure and function of the metal-binding protein S100B and its interaction with the receptor for advanced glycation end products

Autor:	Ostendorp, Thorsten
Jazyk:	angličtina
Rok vydání:	2006
Předmět:	S100-Proteine Zinc Alzheimer-Krankheit [gnd] Kalzium ddc:570 Protein-structure Pichia [gnd] Zink Calcium S100B RAGE Proteinstruktur S100
Popis:	S100B is one of the most abundant proteins in the brain and exerts intra- as well as extracellular functions. It has been implicated to play a key role in many neurodegenerative diseases. Earlier studies showed that these functions might be controlled in a Ca2+ and / or Zn2+ dependent manner. A crucial step in the pathogenesis of neurodegenerative diseases is the activation of the cell surface receptor RAGE by extracellular S100B. Currently, only two NMR structures of human Ca2+ -S100B has been described: dimeric S100B and a complex with the peptide TRTK12. Furthermore only one crystal structure of bovine S100B has been solved so far, but there is no crystal structure of human S100B. The focus and scope of this doctoral thesis was to collect more structural information on the human S100B protein and to investigate the interaction of S100B with its receptor RAGE.
Databáze:	OpenAIRE
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