New Controls for Structure Viewer

The ability to select structures to view in the center window has become easier to manipulate. When you select a collection in the left window, the structures in that collection will become listed in the center window. Previously, you were only able to select structures to see in the viewer by individually clicking the eye icon to the left of the structure.

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We have introduced multi-select to the collections panel, so many checkboxes can be checked with the same ***click + shift-click*** shortcut that can be used in the structure viewer. Now, you will also be able to send structures to the viewer by clicking a new eye icon found above that list of structures in the center window.

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You can check one or more structure boxes, click the new eye icon, then select “Add to Structure Viewer” from the drop down menu to bring selected structures into the viewer. You can also select structures to be removed from the structure viewer or replace structures with a different set.

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One final change is that clicking a structure row will now select or deselect the structure box rather than effect whether its eye icon is active.

Cyrus Scientist Amanda Duran contributes to molecular models studying the mechanisms of mutations in KCNQ1

Abstract: Mutations that induce loss of function (LOF) or dysfunction of the human KCNQ1 channel are responsible for susceptibility to a life-threatening heart rhythm disorder, the congenital long QT syndrome (LQTS). Hundreds of KCNQ1 mutations have been identified, but the molecular mechanisms responsible for impaired function are poorly understood. We investigated the impact of 51 KCNQ1 variants with mutations located within the voltage sensor domain (VSD), with an emphasis on elucidating effects on cell surface expression, protein folding, and structure. For each variant, the efficiency of trafficking to the plasma membrane, the impact of proteasome inhibition, and protein stability were assayed. The results of these experiments combined with channel functional data provided the basis for classifying each mutation into one of six mechanistic categories, highlighting heterogeneity in the mechanisms resulting in channel dysfunction or LOF. More than half of the KCNQ1 LOF mutations examined were seen to destabilize the structure of the VSD, generally accompanied by mistrafficking and degradation by the proteasome, an observation that underscores the growing appreciation that mutation-induced destabilization of membrane proteins may be a common human disease mechanism. Finally, we observed that five of the folding-defective LQTS mutant sites are located in the VSD S0 helix, where they interact with a number of other LOF mutation sites in other segments of the VSD. These observations reveal a critical role for the S0 helix as a central scaffold to help organize and stabilize the KCNQ1 VSD and, most likely, the corresponding domain of many other ion channels.

https://advances.sciencemag.org/content/4/3/eaar2631

(Science Advances  07 Mar 2018: Vol. 4, no. 3, eaar2631)