منابع مشابه
Type II Cadherin Ectodomain Structures: Implications for Classical Cadherin Specificity
Type I and II classical cadherins help to determine the adhesive specificities of animal cells. Crystal-structure determination of ectodomain regions from three type II cadherins reveals adhesive dimers formed by exchange of N-terminal beta strands between partner extracellular cadherin-1 (EC1) domains. These interfaces have two conserved tryptophan side chains that anchor each swapped strand, ...
متن کاملSegregation of VE-cadherin from the LBRC depends on the ectodomain sequence required for homophilic adhesion.
The lateral border recycling compartment (LBRC) is a reticulum ofperijunctional tubulovesicular membrane that is continuous with the plasmalemma of endothelial cells and is essential for efficient transendothelial migration (TEM) of leukocytes. The LBRC contains molecules involved in TEM, such as PECAM, PVR and CD99, but not VE-cadherin. Despite its importance, how membrane proteins are include...
متن کاملLateral clustering of the adhesive ectodomain: a fundamental determinant of cadherin function
BACKGROUND Classical cadherin-based cellular adhesion is mediated by a multicomponent protein complex that links the adhesive binding activity of the cadherin ectodomain to the actin cytoskeleton. Despite the importance of cadherins in morphogenesis and development, we know very little about how cells determine and alter cadherin adhesive strength. In this study, we sought to identify specific ...
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Some of the most important potential applications of carbon nanotubes are related to their mechanical properties. Stiff sp2 bonds result in a Young's modulus close to that of diamond, while the relatively weak van der Waals interaction between the graphitic shells acts as a form of lubrication. Previous characterization of the mechanical properties of nanotubes includes a rich variety of experi...
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The active site of the Haloalkane Dehydrogenase (HaloTag) enzyme can be covalently attached to a chloroalkane ligand providing a mechanically strong tether, resistant to large pulling forces. Here we demonstrate the covalent tethering of protein L and I27 polyproteins between an atomic force microscopy (AFM) cantilever and a glass surface using HaloTag anchoring at one end and thiol chemistry a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.170399