Cadherin
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <StructureSection load='2a4c' size='350' side='right' scene='41/417481/Cv/ | + | <StructureSection load='2a4c' size='350' side='right' scene='41/417481/Cv/4' caption='Mouse cadherin-11 EC1 dimer (PDB code [[2a4c]])'> |
== Function == | == Function == | ||
| Line 8: | Line 8: | ||
== 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 strand swapping is enhanced by <scene name='41/417481/Cv/ | + | 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 <scene name='41/417481/Cv/5'>2 Trp residues</scene> docking into the hydrophobic pocket of the neighboring CDH molecule. <ref>PMID:16564015</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 11:11, 8 January 2019
| |||||||||||
3D Structures of Cadherin
Updated on 08-January-2019
References
- ↑ Angst BD, Marcozzi C, Magee AI. The cadherin superfamily: diversity in form and function. J Cell Sci. 2001 Feb;114(Pt 4):629-41. PMID:11171368
- ↑ Patel SD, Ciatto C, Chen CP, Bahna F, Rajebhosale M, Arkus N, Schieren I, Jessell TM, Honig B, Price SR, Shapiro L. Type II cadherin ectodomain structures: implications for classical cadherin specificity. Cell. 2006 Mar 24;124(6):1255-68. PMID:16564015 doi:http://dx.doi.org/10.1016/j.cell.2005.12.046
