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J Biol Chem

Title:		Structure of Saccharomyces cerevisiae alpha-agglutinin. Evidence for a yeast cell wall protein with multiple immunoglobulin-like domains with atypical disulfides
Author(s):		Chen MH; Shen ZM; Bobin S; Kahn PC; Lipke PN;
Address:		"Department of Biological Sciences, Hunter College of the City University of New York, New York 10021, USA"
Journal Title:		J Biol Chem
Year:		1995
Volume:		270
Issue:		44
Page Number:		26168 - 26177
DOI:		10.1074/jbc.270.44.26168
ISSN/ISBN:		0021-9258 (Print) 0021-9258 (Linking)
Abstract:		"alpha-Agglutinin of Saccharomyces cerevisiae is a cell wall-associated protein that mediates cell interaction in mating. Although the mature protein includes about 610 residues, the NH2-terminal half of the protein is sufficient for binding to its ligand a-agglutinin. alpha-Agglutinin20-351, a fully active fragment of the protein, has been purified and analyzed. Circular dichroism spectroscopy, together with sequence alignments, suggest that alpha-agglutinin20-351 consists of three immunoglobulin variable-like domains: domain I, residues 20-104; domain II, residues 105-199; and domain III, residues 200-326. Peptide sequencing data established the arrangement of the disulfide bonds in alpha-agglutinin20-351. Cys97 is disulfide-bonded to Cys114, forming an interdomain bond between domains I and II. Cys202 is bonded to Cys300, in an atypical intradomain disulfide bond between the A and F strands of domain III. Cys227 and Cys256 have free sulfhydryls. Sequencing also showed that at least two of three potential N-glycosylation sites with sequence Asn-Xaa-Thr are glycosylated. At least one of three Asn-Xaa-Ser sequences is not glycosylated. No residues NH2-terminal to Ser282 were O-glycosylated, whereas Ser282, and all hydroxy amino acid residues COOH-terminal to this position were modified. Therefore O-glycosylated Ser and Thr residues cluster in the COOH-terminal region of domain III, and the O-glycosylation continues into a Ser/Thr-rich sequence that extends from domain III to the COOH-terminal of the full-length protein"
Keywords:		Agglutinins/chemistry Amino Acid Sequence Base Sequence Circular Dichroism Consensus Sequence DNA Primers Immunoglobulin Variable Region/chemistry Immunoglobulins/chemistry Mating Factor Molecular Sequence Data Peptide Biosynthesis Peptide Fragments/chemi;
Notes:		"MedlineChen, M H Shen, Z M Bobin, S Kahn, P C Lipke, P N eng Comparative Study Research Support, U.S. Gov't, P.H.S. 1995/11/03 J Biol Chem. 1995 Nov 3; 270(44):26168-77. doi: 10.1074/jbc.270.44.26168"