학술논문
Kinetic intermediates in the reactions between peptides and proteins of major histocompatibility complex class II.
Document Type
Article
Author
Source
Proceedings of the National Academy of Sciences of the United States of America; September 1994, Vol. 91 Issue: 19 p8842-8845, 4p
Subject
Language
ISSN
00278424; 10916490
Abstract
The kinetics of the reactions between fluorescently labeled sperm whale myoglobin-(110-121) peptide and the murine major histocompatibility complex class II protein I-Ed have been analyzed. The presence in solution of both short- and long-lived protein-peptide complexes is demonstrated by the biphasic dissociation of the myoglobin peptide from I-Ed. The formation of the long-lived terminal complex is preceded by a characteristic induction phase. It is shown that the initially formed complex of the myoglobin peptide and I-Ed is a kinetic intermediate that undergoes a unimolecular reaction to form the terminal complex. Reactions between peptides and the class II proteins thus involve an intermediate structurally distinct from the terminal complex. The terminal complex presumably has a structure that is biologically active and similar to the published class II protein-peptide crystal structure.