Structural analysis of the murine cell adhesion molecule L1 by electron microscopy and computer-assisted modelling

The European Journal of Neuroscience
B DrescherR Probstmeier

Abstract

In the present study we have analysed the morphology of two fragments with apparent molecular weights of 180 and 140 kDA (L1-180 and L1-140) derived from the extracellular region of the murine neural cell adhesion molecule L1. The fragment L1-180 consists of almost the entire extracellular part of the molecule, and is built up of six immunoglobulin-like and five fibronectin type III-like domains. Fragment L1-140 lacks one-half of the third, the fourth and the fifth fibronectin type III-like domains. By electron microscopic analysis of rotary-shadowed molecules, L1-140 and L1-180 revealed fibrillar structures 31-43 nm long and 7-12 nm wide with one pronounced globular terminal domain. As determined by complex formation with an L1 antibody, this terminal part of the molecule is formed by the fibronectin type III-like domains. The individual structures showed variation and complexity, and four distinct aspects were identified. These different forms probably represent two-dimensional projections of the same three-dimensional helical structure. Computer-assisted modelling of the L1 molecule, i.e. the protein backbone, showed no strong intramolecular interaction between the different fibronectin type III- or Ig-like domains, suggesti...Continue Reading

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May 6, 1998·Current Opinion in Neurobiology·T BrümmendorfF G Rathjen
Jun 16, 2001·Molecular Biology of the Cell·G SchürmannH P Erickson
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Jan 24, 2021·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Gabriele LoersMelitta Schachner

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