The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications.

• DOI: 10.1073/pnas.90.22.10783
• Publication Date: 2006-05-31T12:36:02Z
• Authors: T G Wolfsberg; J F Bazan; C P Blobel; D G Myles; P Primakoff; J M White
• Keywords: Male; 0303 health sciences; Membrane Glycoproteins; Disintegrins; Molecular Sequence Data; Gene Expression; Membrane Proteins; Metalloendopeptidases; Proteins; 3. Good health; ADAM Proteins; 03 medical and health sciences; Fertilins; Cricetinae; Animals; Female; Amino Acid Sequence; RNA, Messenger; Cloning, Molecular; Protein Precursors; Peptides; Sequence Alignment; Phylogeny

PH-30, a sperm surface protein involved in sperm-egg fusion, is composed of two subunits, alpha and beta, which are synthesized as precursors processed, during development, to yield the mature forms. The PH-30 alpha/beta complex resembles certain viral fusion proteins membrane topology predicted binding functions. Furthermore, subunits similar sequence each other family disintegrin domain-containing snake venom proteins. We report here sequences beta precursor regions. Their domain organizations metalloproteases disintegrins. region contains, from amino carboxyl terminus, pro, metalloprotease, domains. contains pro metalloprotease Residues diagnostic catalytically active present alpha, but not region. propose that sites structurally astacin. acting through its and/or domains, could be development well fusion. Phylogenetic analysis indicates stems multidomain ancestral protein.