Dynamics and stability of E-cadherin dimers.

@article{citeulike:2755144, abstract = {The extracellular domains of cadherins are known to play a major role in cell adhesion, although the structures involved in this process remain unclear. We have used molecular dynamics to characterize the conformational and thermodynamic properties of two of the dimer interfaces identified in E-cadherin crystals and involving the two outermost exodomains (EC1 and EC2): a dimer involving exchange of the N-terminal strand (referred to as the "swapped" dimer) and a "staggered" dimer involving an EC1-EC2 interface. The results show that the staggered dimer involves a much smaller interface area and is notably less stable than the swapped dimer. It is also found that, despite its stability, the swapped dimer undergoes a conformational transition leading to a structure closer to that experimentally observed for the homologous C-cadherin. Finally, comparing the simulated dimer structures with the sequences of E-, C-, and N-cadherins shows that the swapped dimer interface involves surprisingly few residues that vary from family to family and notably no changes between the E- and C-cadherin exodomains.}, address = {Laboratoire de Biochimie Th\'{e}orique, CNRS UPR 9080, Institut de Biologie Physico-Chimique, Paris, France.}, author = {Cailliez, F. and Lavery, R. }, citeulike-article-id = {2755144}, comment = {MD study using AMBER 8}, doi = {10.1529/biophysj.106.087213}, issn = {0006-3495}, journal = {Biophysical journal}, keywords = {cell-adhesion}, month = {December}, number = {11}, pages = {3964--3971}, posted-at = {2008-05-05 05:47:45}, priority = {2}, title = {Dynamics and stability of E-cadherin dimers.}, url = {http://dx.doi.org/10.1529/biophysj.106.087213}, volume = {91}, year = {2006} }

TY - JOUR ID - citeulike:2755144 L3 - citeulike-article-id:2755144 TI - Dynamics and stability of E-cadherin dimers. JF - Biophysical journal VL - 91 IS - 11 SP - 3964 EP - 3971 AD - Laboratoire de Biochimie Théorique, CNRS UPR 9080, Institut de Biologie Physico-Chimique, Paris, France. SN - 0006-3495 N2 - The extracellular domains of cadherins are known to play a major role in cell adhesion, although the structures involved in this process remain unclear. We have used molecular dynamics to characterize the conformational and thermodynamic properties of two of the dimer interfaces identified in E-cadherin crystals and involving the two outermost exodomains (EC1 and EC2): a dimer involving exchange of the N-terminal strand (referred to as the "swapped" dimer) and a "staggered" dimer involving an EC1-EC2 interface. The results show that the staggered dimer involves a much smaller interface area and is notably less stable than the swapped dimer. It is also found that, despite its stability, the swapped dimer undergoes a conformational transition leading to a structure closer to that experimentally observed for the homologous C-cadherin. Finally, comparing the simulated dimer structures with the sequences of E-, C-, and N-cadherins shows that the swapped dimer interface involves surprisingly few residues that vary from family to family and notably no changes between the E- and C-cadherin exodomains. KW - cell-adhesion N1 - MD study using AMBER 8 AU - Cailliez, F AU - Lavery, R PY - 2006/12/01/ UR - http://dx.doi.org/10.1529/biophysj.106.087213 ER -