Extreme convergent evolution in defensin proteins & quantitative maps of their sequence space

Shafee, Thomas; Lay, Fung T.; Hulett, Mark D.; ANDERSON, MARILYN

doi:10.26181/5e5b7468351b0

2016 SMBE Convergence poster.pdf (1.76 MB)

Extreme convergent evolution in defensin proteins & quantitative maps of their sequence space

poster

posted on 2020-03-01, 08:37 authored by Thomas Shafee, Fung T. Lay, Mark D. Hulett, MARILYN ANDERSON

Poster presented at

SMBE 2016

Gordon AMPs 2017

Defensins are small, charged, disulphide-rich

eukaryotic proteins with diverse sequences, structures, and

functions. Their antimicrobial activities are of particular interest

for protecting crops and humans from pathogens.

They have been traditionally treated as a single superfamily.

However, we present evidence that there exist two independent

evolutionary origins of defensins, based on their secondary

structure element order, disulphide topology, and tertiary

structures. These two superfamilies, the cis-defensins and transdefensins,

exhibit some of the most extensive convergent

evolution of protein sequence, structure and function.

We have developed new methods of sequence alignment and

analysis to overcome the difficulties of investigating such short

and divergent sequences. Multivariate analysis of protein

sequence space allows grouping of defensins into naturally

occurring clusters which describe the residue properties that

separate phyla and functions. It can be further used to design

synthetic, cluster-central, archetypal defensin sequences.

History

First created date

2016-04-01

School

School of Molecular Sciences

Publication Date

2016-04-01

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