Cadherin: Difference between revisions
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<StructureSection load='2a4c' size='450' side='right' scene= caption='Lymnaea acetylcholine-binding protein pentamer complex with acetylcholine (PDB code 3wip)'> | <StructureSection load='2a4c' size='450' side='right' scene= caption='Lymnaea acetylcholine-binding protein pentamer complex with acetylcholine (PDB code 3wip)'> | ||
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
The adhesive binding of CDH arises from the exchange of β strand of one CDH with the strand of CDH of a neighboring cell termed ''strand swap''. | The adhesive binding of CDH arises from the exchange of β strand of one CDH with the strand of CDH of a neighboring cell termed ''strand swap''. The strand swapping is enhanced by 2 Trp residues docking into the hydrophobic pocket of the neighboring CDH molecule. | ||
</StructureSection> | </StructureSection> |
Revision as of 12:52, 16 November 2015
FunctionCadherins (CDH) are calcium-dependent adhesion proteins. They contain extracellular CDH repeats (EC1-EC5) which bind calcium ions. They are encoded by numerous genes numbered CDH1-CDH23. Some names of CDH indicate their locations: E-CDH (epithelial tissue), VE-CDH (vascular epithelial), T-CDH bound to membrane, N-CDH (neurons), P-CDH (placental). The CDH superfamily contains:
Structural highlightsThe adhesive binding of CDH arises from the exchange of β strand of one CDH with the strand of CDH of a neighboring cell termed strand swap. The strand swapping is enhanced by 2 Trp residues docking into the hydrophobic pocket of the neighboring CDH molecule.
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3D Structures of Cadherin3D Structures of Cadherin
Updated on 16-November-2015