English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance The fertilization of eggs by sperm is a critical biological process for nearly all sexually reproducing organisms to propagate their genetic information, yet the molecules that mediate egg−sperm interactions evolve at extraordinary rates, and their biochemical mechanisms are poorly understood. In the marine mollusk abalone, sperm lysin interacts with egg vitelline envelope receptor for lysin (VERL) in a species-specific manner to facilitate fertilization. In this report, we characterized the solution structure and molecular evolution of sperm lysin from red abalone (Haliotis rufescens ), and identified that the VERL binding interface has experienced incessant sexual coevolution. Furthermore, increased dynamics in the lysin fold has facilitated this exacerbated evolution, and may reflect a common molecular basis for accelerated evolution in other rapidly evolving proteins, such as immune genes.

Solution structure of sperm lysin yields novel insights into molecular dynamics of rapid protein evolution