< Terug naar vorige pagina

Publicatie

Comparative sequence and structural analyses of neuroserpin – the serine protease inhibitor family

Boekbijdrage - Boekhoofdstuk Conferentiebijdrage

Neuroserpin clade of serpins is a family of serine protease inhibitors (>220 residues), and is a selective inhibitor of tissue-type plasminogen activator (tPA). The crystal structure of native human neuroserpin has been reported by Sayaka et al., at 2.1 Å resolution. The native fold consists of a five stranded β-sheet A and a mobile helical reactive center loop. The structure also has an omega loop, which contributes to the inhibition of tPA. In this study, we aim to identify new members of the neuroserpin family by comparative sequence analyses and we investigate the conservation of the reactive center loop (RCL), the omega loop (Ω-loop), the helix „F‟ and other consensus residues, in the newly found relatives, which differ from the consensus sequences of other clades of serpins. By comparative structural analyses of the structurally similar proteins of neuroserpin, we find structural patterns and stabilizing interactions that are unique among the members of neuroserpin family.
Boek: In Proceedings of the international Symposium on Biocomputing (Calicut, Kerala, India, February 15 - 17, 2010). ISB '10.
Pagina's: 1 - 7
ISBN:9781605587226
Jaar van publicatie:2010
Toegankelijkheid:Closed