Molecular dissection of the CD2-CD58 counter-receptor interface identifies CD2 Tyr86 and CD58 Lys34 residues as the functional "hot spot".

doi:10.1006/jmbi.2001.4980

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Article

Molecular dissection of the CD2-CD58 counter-receptor interface identifies CD2 Tyr86 and CD58 Lys34 residues as the functional "hot spot".

Journal of molecular biology - 28 Sept 2001

Kim M, Sun Z Y, Byron O, Campbell G, Wagner G, Wang J, Reinherz E L

Abstract excerpt

The heterophilic CD2-CD58 adhesion interface contains interdigitating residues that impart high specificity and rapid binding kinetics. To define the hot spot of this counter-receptor interaction, we characterized CD2 adhesion domain variants harboring a single mutation of the central Tyr86 or of each amino acid residue forming a salt link/hydrogen bond. Alanine mutations at D31, D32 and K34 on the C strand and...

Topics

Amino Acid Substitution
Animals
Binding Sites
CD2 Antigens
CD58 Antigens
Calorimetry
Cell Adhesion
Chromatography, Gel
Erythrocytes
Humans
Hydrogen Bonding
Inhibitory Concentration 50
Jurkat Cells
Lysine

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Magnetic Resonance Spectroscopy

Models, Molecular

Mutation

Protein Binding

Source

Open in PubMed

Identifiers

PMID: 11575926
DOI: 10.1006/jmbi.2001.4980

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