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Ancestral Sequence Reconstruction$
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David A Liberles

Print publication date: 2007

Print ISBN-13: 9780199299188

Published to Oxford Scholarship Online: September 2008

DOI: 10.1093/acprof:oso/9780199299188.001.0001

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Linking sequence to function in drug design with ancestral sequence reconstruction

Linking sequence to function in drug design with ancestral sequence reconstruction

Chapter:
(p.34) CHAPTER 3 Linking sequence to function in drug design with ancestral sequence reconstruction
Source:
Ancestral Sequence Reconstruction
Author(s):

Janos T. Kodra

Marie Skovgaard

Dennis Madsen

David A. Liberles

Publisher:
Oxford University Press
DOI:10.1093/acprof:oso/9780199299188.003.0003

Many bioactive peptides and proteins of pharmaceutical interest are found in animal venoms. Nature often reuses scaffolds within protein frameworks to develop new properties. The binding core of the peptide from venomous animals is conserved through species (built on a small number of permissive scaffolds). The same scaffolds are often found in nature in protein, performing other non-toxic functions, and it is likely that such conserved motifs are the result of divergent evolution from a common ancestor protein framework via gene duplication. This chapter describes the use of ancestral sequence reconstruction to identify and reconstruct the evolutionary history of important physiological protein and peptide and to connect their common ancestor to certain venom peptides and proteins. This process helps with identifying which amino acids are important for functioning and which ultimately can be used to engineer new bioactive peptide with tailor made properties.

Keywords:   venom peptides, venom proteins, protein engineering, coagulation factors, scaffolds, gene duplication

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