1spp
THE CRYSTAL STRUCTURES OF TWO MEMBERS OF THE SPERMADHESIN FAMILY REVEAL THE FOLDING OF THE CUB DOMAINTHE CRYSTAL STRUCTURES OF TWO MEMBERS OF THE SPERMADHESIN FAMILY REVEAL THE FOLDING OF THE CUB DOMAIN
Structural highlights
FunctionPSP1_PIG Not yet identified, major porcine seminal plasma protein. Can bind soybean trypsin inhibitor after deglycosylation. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSpermadhesins, 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. The crystal structures of two spermadhesins reveal the CUB domain fold.,Romero A, Romao MJ, Varela PF, Kolln I, Dias JM, Carvalho AL, Sanz L, Topfer-Petersen E, Calvete JJ Nat Struct Biol. 1997 Oct;4(10):783-8. PMID:9334740[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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