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== Abstract == | == Abstract == | ||
[[Fascin 1 | Back to main page]] | Investigation into the human fascin-1 protein was undertaken to understand its evolutionary history as well as its structural & functional properties. High sequence identity was found across multiple different eukaryotic species. Structuraly similar proteins were found to have very little sequence identity and no functional relationship to actin-binding protein fascin. | ||
The two actin-binding regions of fascin were narrowed down to the the N-terminal region and C-terminal region of fascin which is conserved throughout different species studied to date. Although exact binding region is still unknown, we present that it encompasses residues 136-143 and 386-395 at the N and C terminals respectively. | |||
[[Fascin Abstract | Abstract]] | [[Fascin Introduction | Introduction]] | [[Fascin Methods | Methods]] | [[Fascin Results | Results]] | [[Fascin Discussion | Discussion]] | [[Fascin Conclusion | Conclusion]] | [[Fascin References | References]] | |||
<br>[[Fascin 1 | Back to Fascin main page]] |
Latest revision as of 01:45, 16 June 2009
Abstract
Investigation into the human fascin-1 protein was undertaken to understand its evolutionary history as well as its structural & functional properties. High sequence identity was found across multiple different eukaryotic species. Structuraly similar proteins were found to have very little sequence identity and no functional relationship to actin-binding protein fascin.
The two actin-binding regions of fascin were narrowed down to the the N-terminal region and C-terminal region of fascin which is conserved throughout different species studied to date. Although exact binding region is still unknown, we present that it encompasses residues 136-143 and 386-395 at the N and C terminals respectively.
Abstract | Introduction | Methods | Results | Discussion | Conclusion | References
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