1999Unpublished venueRequires access

STRUCTURAL FEATURES OF NEURAL IMMUNOGLOBULIN SUPERFAMILY ADHESION MOLECULES

Christoph Rader, P. Sonderegger

Open publisher page 2 citations

Abstract

Neural cell adhesion molecules containing domains resembling the domains of the immunoglobulins (Ig domains) play a major role in the specific cellular recognition processes that are fundamental for the developmental migration of cells, the formation and guidance of axons, and the specific and reproducible formation of synaptic connections. The Ig domains, which represent the common structural element of the Ig superfamily molecules, have a characteristic fold of their peptide chains and, in all cases where a molecular function has been determined, they mediate specific contacts with other molecules at the cellular surface of the same or other cells. Recent developments indicate that cellular contacts mediated by Ig superfamily cell adhesion molecules may also elicit intracellular signals and the Ig domain has been found as an element of the extracellular portion of many trans-membrane receptor proteins. The first chapter of this book is aimed at describing the structural features of the Ig fold and its binding function.

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Neural cell adhesion molecules containing domains resembling the domains of the immunoglobulins (Ig domains) play a major role in the specific cellular recognition processes that are fundamental for the developmental migration of cells, the formation and guidance of axons, and the specific and reproducible formation of synaptic connections. The Ig domains, which represent the common structural element of the Ig superfamily molecules, have a characteristic fold of their peptide chains and, in all cases where a molecular function has been determined, they mediate specific contacts with other molecules at the cellular surface of the same or other cells. Recent developments indicate that cellular contacts mediated by Ig superfamily cell adhesion molecules may also elicit intracellular signals and the Ig domain has been found as an element of the extracellular portion of many trans-membrane receptor proteins. The first chapter of this book is aimed at describing the structural features of the Ig fold and its binding function.

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Available abstract

Neural cell adhesion molecules containing domains resembling the domains of the immunoglobulins (Ig domains) play a major role in the specific cellular recognition processes that are fundamental for the developmental migration of cells, the formation and guidance of axons, and the specific and reproducible formation of synaptic connections. The Ig domains, which represent the common structural element of the Ig superfamily molecules, have a characteristic fold of their peptide chains and, in all cases where a molecular function has been determined, they mediate specific contacts with other molecules at the cellular surface of the same or other cells. Recent developments indicate that cellular contacts mediated by Ig superfamily cell adhesion molecules may also elicit intracellular signals and the Ig domain has been found as an element of the extracellular portion of many trans-membrane receptor proteins. The first chapter of this book is aimed at describing the structural features of the Ig fold and its binding function.

Key concepts: Immunoglobulin superfamily, SUPERFAMILY, Neural cell adhesion molecule, Cell adhesion molecule, Adhesion, Antibody, Computational biology, Chemistry

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