期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1774, 期 9, 页码 1148-1155出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2007.06.014
关键词
integrin; metal ion; LFA-1; ICAM-1; isothermal calorimetry; surface plasmon resonance
资金
- NCI NIH HHS [R37 CA031798-27, R01 CA031798, CA31798, R37 CA031798] Funding Source: Medline
- NIAID NIH HHS [R01 AI072765] Funding Source: Medline
Integrins are cell-surface heterodimeric proteins that mediate cell-cell, cell-matrix, and cell-pathogen interactions. Half of the known integrin a subunits contain inserted domains (I domains) that coordinate ligand through a metal ion. Although the importance of conformational changes within isolated I domains in regulating ligand binding has been reported, the relationship between metal ion binding affinity and ligand binding affinity has not been elucidated. Metal and ligand binding by several I domain mutants that are stabilized in different conformations are investigated using isothermal titration calorimetry and surface plasmon resonance studies. This work suggests an inverse relationship between metal ion affinity and ligand binding affinity (i.e. constructs with a high affinity for ligand exhibit a low affinity for metal). This trend is discussed in the context of structural studies to provide an understanding of interplay between metal ion binding and ligand affinities and conformational changes. (c) 2007 Elsevier B.V. All rights reserved.
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