Prediction of the protein folding core: Application to the immunoglobulin fold

Biochimie ◽  
2009 ◽  
Vol 91 (11-12) ◽  
pp. 1465-1474 ◽  
Author(s):  
Nicolas Prudhomme ◽  
Jacques Chomilier
Keyword(s):  
Protein Folding ◽  
Immunoglobulin Fold

scholarly journals Residues on Both Faces of the First Immunoglobulin Fold Contribute to Homophilic Binding Sites of PECAM-1/CD31

1997 ◽  
Vol 272 (33) ◽  
pp. 20555-20563 ◽  
Author(s):  
Justin P. Newton ◽  
Christopher D. Buckley ◽  
E. Yvonne Jones ◽  
David L. Simmons
Keyword(s):  
Binding Sites ◽  
Homophilic Binding ◽  
Immunoglobulin Fold

scholarly journals A regulatable switch mediates self-association in an immunoglobulin fold

2008 ◽  
Vol 15 (9) ◽  
pp. 965-971 ◽  
Author(s):  
Matthew F Calabrese ◽  
Catherine M Eakin ◽  
Jimin M Wang ◽  
Andrew D Miranker
Keyword(s):  
Self Association ◽  
Immunoglobulin Fold

The Immunoglobulin Fold

1994 ◽  
Vol 242 (4) ◽  
pp. 309-320 ◽  
Author(s):  
P. Bork ◽  
L. Holm ◽  
C. Sander
Keyword(s):  
Immunoglobulin Fold

scholarly journals Identification of a ligand-binding site in an immunoglobulin fold domain of the Saccharomyces cerevisiae adhesion protein alpha-agglutinin.

1996 ◽  
Vol 7 (1) ◽  
pp. 143-153 ◽  
Author(s):  
H de Nobel ◽  
P N Lipke ◽  
J Kurjan
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ligand Binding ◽  
Binding Site ◽  
Mutational Analysis ◽  
Homology Model ◽  
Ligand Binding Site ◽  
Adhesion Protein ◽  
Interaction Sites ◽  
Critical Residue ◽  
Immunoglobulin Fold

The Saccharomyces cerevisiae adhesion protein alpha-agglutinin (Ag alpha 1p) is expressed by alpha cells and binds to the complementary a-agglutinin expressed by a cells. The N-terminal half of alpha-agglutinin is sufficient for ligand binding and has been proposed to contain an immunoglobulin (Ig) fold domain. Based on a structural homology model for this domain and a previously identified critical residue (His292), we made Ag alpha 1p mutations in three discontinuous patches of the domain that are predicted to be in close proximity to His292 in the model. Residues in each of the three patches were identified that are important for activity and therefore define a putative ligand binding site, whereas mutations in distant loops had no effect on activity. This putative binding site is on a different surface of the Ig fold than the defined binding sites of immunoglobulins and other members of the Ig superfamily. Comparison of protein interaction sites by structural and mutational analysis has indicated that the area of surface contact is larger than the functional binding site identified by mutagenesis. The putative alpha-agglutinin binding site is therefore likely to identify residues that contribute to the functional binding site within a larger area that contacts a-agglutinin.

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