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Engineered epidermal growth factor mutants with faster binding on-rates correlate with enhanced receptor activation.

ABSTRACT: Receptor tyrosine kinases (RTKs) regulate critical cell signaling pathways, yet the properties of their cognate ligands that influence receptor activation are not fully understood. There is great interest in parsing these complex ligand-receptor relationships using engineered proteins with altered binding properties. Here we focus on the interaction between two engineered epidermal growth factor (EGF) mutants and the EGF receptor (EGFR), a model member of the RTK superfamily. We found that EGF mutants with faster kinetic on-rates stimulate increased EGFR activation compared to wild-type EGF. These findings support previous predictions that faster association rates correlate with enhanced receptor activity.

SUBMITTER: Lahti JL

PROVIDER: S-EPMC3118396 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Engineered epidermal growth factor mutants with faster binding on-rates correlate with enhanced receptor activation.

Lahti Jennifer L JL Lui Bertrand H BH Beck Stayce E SE Lee Stephen S SS Ly Daphne P DP Longaker Michael T MT Yang George P GP Cochran Jennifer R JR

FEBS letters 20110323 8

Receptor tyrosine kinases (RTKs) regulate critical cell signaling pathways, yet the properties of their cognate ligands that influence receptor activation are not fully understood. There is great interest in parsing these complex ligand-receptor relationships using engineered proteins with altered binding properties. Here we focus on the interaction between two engineered epidermal growth factor (EGF) mutants and the EGF receptor (EGFR), a model member of the RTK superfamily. We found that EGF m ...[more]

PMID: 21439278

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Dataset Information

Engineered epidermal growth factor mutants with faster binding on-rates correlate with enhanced receptor activation.

Publications

Engineered epidermal growth factor mutants with faster binding on-rates correlate with enhanced receptor activation.

Similar Datasets

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