Investigating extracellular in situ EGFR structure and conformational changes using FRET microscopy.

Biochem Soc Trans

Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, Oxon OX11 0QX, UK.

Published: February 2012

AI Article Synopsis

  • * Structural models of entire receptors help predict how these enzymes are regulated, but some predictions don't match experimental cell data.
  • * This disparity highlights the necessity of studying complete ErbB proteins through both cellular experiments and structural analysis for a comprehensive understanding.*

Article Abstract

The crystallographic structures of functional fragments of ErbBs have provided excellent insights into the geometry of growth factor binding and receptor dimerization. By placing together receptor fragments to build structural models of entire receptors, we expect to understand how these enzymes are allosterically regulated; however, several predictions from these models are inconsistent with experimental evidence from cells. The opening of this gap underlines the need to investigate intact ErbBs by combining cellular and structural studies into a full picture.

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Source
http://dx.doi.org/10.1042/BST20110632DOI Listing

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