Immunoglobulin superfamily cell adhesion molecules: zippers and signals.
The latest structural studies of immunoglobulin superfamily cell adhesion molecules are driving a shift in perspective; increasingly the view is not focused solely on the individual molecule but rather is on the molecular assembly. Two common themes are emerging, revealing mechanisms for ectodomain-dependent regulation of cell surface receptors' signalling abilities. The first is the propensity of many such molecules to arrange in zipper-type or array-type assemblies driven by a network of highly specific cis and trans interactions. The second is the use of the extracellular dimensions of a molecule or adhesion complex as properties which, in combination with characteristic intercellular spacings, can determine the co-localisation or exclusion of particular protein populations at cell interfaces and junctions.
Aricescu
A Radu
AR
Cancer Research UK Receptor Structure Research Group, Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Roosevelt Drive, Headington, Oxford OX3 7BN, UK.
Jones
E Yvonne
EY
D000818:Animals; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007136:Immunoglobulins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D015398:Signal Transduction / Q000502:physiology
D015815:Cell Adhesion Molecules; D007136:Immunoglobulins; D011134:Polysaccharides