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The crystal structures of two spermadhesins reveal the CUB domain fold.

Nat. Struct. Biol.1997 Oct;4(10):783-8. doi:10.1038/nsb1097-783
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摘要


Spermadhesins, 12,000-14,000 M(r) mammalian proteins, include lectins involved in sperm-egg binding and display a single CUB domain architecture. We report the crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two glycosylated spermadhesins, and bovine aSFP at 2.4 A and 1.9 A resolution respectively.

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