Solution structure of a peptide derived from the β subunit of LFA-1
| Autor: | Wong S. Ying, Seetharama D. Jois, Zhang Shuxing, Teruna J. Siahaan |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Magnetic Resonance Spectroscopy
Protein Conformation Physiology Stereochemistry Protein subunit Peptide Biochemistry Cellular and Molecular Neuroscience Endocrinology Antigen Cell Adhesion Molecule chemistry.chemical_classification Molecular Structure Circular Dichroism Adhesion Intercellular adhesion molecule Lymphocyte Function-Associated Antigen-1 Peptide Fragments Cyclic peptide Peptide Conformation Solutions Protein Subunits chemistry Protein Binding |
| Zdroj: | Peptides. 24:827-835 |
| ISSN: | 0196-9781 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect