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.

Abstract

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.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Crystallography, X-Ray
  • Dimerization
  • Female
  • Glycoproteins / chemistry*
  • Glycosylation
  • Macromolecular Substances
  • Male
  • Mammals
  • Models, Structural
  • Molecular Sequence Data
  • Protein Conformation*
  • Protein Folding*
  • Semen / chemistry
  • Seminal Vesicle Secretory Proteins*
  • Sequence Alignment
  • Sperm-Ovum Interactions
  • Swine

Substances

  • Glycoproteins
  • Macromolecular Substances
  • Seminal Vesicle Secretory Proteins
  • seminal vesicle secretory protein II, porcine
  • seminal vesicle secretory protein 109, porcine