ArticleMolecular biology of the cell2001
Cell adhesion molecule L1 in folded (horseshoe) and extended conformations.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 77 citations in OpenAlex.
- The Role of the Immunoglobulin Superfamily of Cell Adhesion Molecules in Intellectual Disability.Cells · 2026Review
- Structural Perspectives on Extracellular Recognition and Conformational Changes of Several Type-I Transmembrane Receptors.Frontiers in molecular biosciences · 2020Review
- Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin Trans-synaptic Bridges.Neuron · 2017Article
- Conditional deletion of L1CAM in human neurons impairs both axonal and dendritic arborization and action potential generation.The Journal of experimental medicine · 2016Article
- An extracellular adhesion molecule complex patterns dendritic branching and morphogenesis.Cell · 2013Article
- The switch-associated protein 70 (SWAP-70) bundles actin filaments and contributes to the regulation of F-actin dynamics.The Journal of biological chemistry · 2013Article
- Regulation of adhesion by flexible ectodomains of IgCAMs.Neurochemical research · 2013Review
- Mitogen-activated protein kinase modulates ethanol inhibition of cell adhesion mediated by the L1 neural cell adhesion molecule.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The secreted immunoglobulin domain proteins ZIG-5 and ZIG-8 cooperate with L1CAM/SAX-7 to maintain nervous system integrity.PLoS genetics · 2012Article
- Two alcohol binding residues interact across a domain interface of the L1 neural cell adhesion molecule and regulate cell adhesion.The Journal of biological chemistry · 2011Article
- Homophilic adhesion mechanism of neurofascin, a member of the L1 family of neural cell adhesion molecules.The Journal of biological chemistry · 2011Article
- L1CAM malfunction in the nervous system and human carcinomas.Cellular and molecular life sciences : CMLS · 2010Review
- Inside-out regulation of L1 conformation, integrin binding, proteolysis, and concomitant cell migration.Molecular biology of the cell · 2010Article
- "CRASH"ing with the worm: insights into L1CAM functions and mechanisms.Developmental dynamics : an official publication of the American Association of Anatomists · 2010Review
- Structural determinants of autoproteolysis of the Haemophilus influenzae Hap autotransporter.Infection and immunity · 2009Article
- Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy.Biological procedures online · 2009Article
- Cryo-electron tomography of homophilic adhesion mediated by the neural cell adhesion molecule L1.Structure (London, England : 1993) · 2009Article
- Effects of ethanol on axon outgrowth and branching in developing rat cortical neurons.Neuroscience · 2008Article
- Kinetic analysis of L1 homophilic interaction: role of the first four immunoglobulin domains and implications on binding mechanism.The Journal of biological chemistry · 2008Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We have investigated the structure of the cell adhesion molecule L1 by electron microscopy. We were particularly interested in the conformation of the four N-terminal immunoglobulin domains, because x-ray diffraction showed that these domains are bent into a horseshoe shape in the related molecules hemolin and axonin-1. Surprisingly, rotary-shadowed specimens showed the molecules to be elongated, with no indication of the horseshoe shape. However, sedimentation data suggested that these domains of L1 were folded into a compact shape in solution; therefore, this prompted us to look at the molecules by an alternative technique, negative stain. The negative stain images showed a compact shape consistent with the expected horseshoe conformation. We speculate that in rotary shadowing the contact with the mica caused a distortion of the protein, weakening the bonds forming the horseshoe and permitting the molecule to extend. We have thus confirmed that the L1 molecule is primarily in the horseshoe conformation in solution, and we have visualized for the first time its opening into an extended conformation. Our study resolves conflicting interpretations from previous electron microscopy studies of L1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.