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The crystal structures of two spermadhesins reveal the CUB domain fold
- Source :
- CIÊNCIAVITAE, Scopus-Elsevier
- Publication Year :
- 1997
-
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.
- Subjects :
- Male
Protein Folding
Glycosylation
Macromolecular Substances
Protein Conformation
Swine
Molecular Sequence Data
Sequence alignment
Crystal structure
Biology
Crystallography, X-Ray
Seminal Vesicle Secretory Proteins
Biochemistry
chemistry.chemical_compound
Protein structure
Structural Biology
Semen
Genetics
Animals
Amino Acid Sequence
Peptide sequence
Seminal Vesicle Proteins
Glycoproteins
Mammals
Sperm-Ovum Interactions
CUB domain
eye diseases
Models, Structural
chemistry
Biophysics
Protein folding
Cattle
Female
Dimerization
Sequence Alignment
Subjects
Details
- ISSN :
- 10728368
- Volume :
- 4
- Issue :
- 10
- Database :
- OpenAIRE
- Journal :
- Nature structural biology
- Accession number :
- edsair.doi.dedup.....e0e90c5856f77b582c953b947fd10999