title: Solution structure of a peptide derived from the beta subunit of LFA-1.
abstract: Cell-adhesion molecules are critical for immune response. It is well known that the inhibition of adhesion is very effective in immunotherapy and that the peptides derived from leukocyte function associated antigen (LFA-1) and intercellular adhesion molecule (ICAM-1) modulate cell-adhesion interaction. The three-dimensional structure of a cyclic peptide, Cyclo(1,12)Pen(1)-Asp(2)-Leu(3)-Ser(4)-Tyr(5)-Ser(6)-Leu(7)-Asp(8)-Asp(9)-Leu(10)-Arg(11)-Cys(12) (cLBEL) derived from the beta subunit of LFA-1 which is known to modulate homotypic T-cell-adhesion process has been studied using NMR, CD and molecular dynamics (MD) simulation. The peptide exhibits two possible conformations in solution. Structure I has a conformation with two consecutive beta-turns involving residues Tyr(5)-Ser(6)-Leu(7)-Asp(8) and Asp(9)-Leu(10)-Arg(11)-Cys(12). Structure II has a beta-turn at Tyr(5)-Ser(6)-Leu(7)-Asp(8) and forms a beta-hairpin type of conformation.
authors.affiliation: Department of Pharmacy, National University of Singapore, 18 Science Drive 4, Singapore 117543, Singapore.
authors.forename: Zhang
authors.initials: Z
authors.lastname: Shuxing
authors.forename: Wong S
authors.initials: WS
authors.lastname: Ying
authors.forename: Teruna J
authors.initials: TJ
authors.lastname: Siahaan
authors.forename: Seetharama D S
authors.initials: SD
authors.lastname: Jois
mesh_terms: D002448:Cell Adhesion; D002942:Circular Dichroism; D016169:Lymphocyte Function-Associated Antigen-1 / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry
chemical_list: D016169:Lymphocyte Function-Associated Antigen-1; D010446:Peptide Fragments; D021122:Protein Subunits; D012996:Solutions