Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Structural and functional analysis of WASP family cell signaling proteins shows that the same residues that are sequestered upon GTPase binding in the autoinhibited state are involved in binding to and activating Arp2/3 complex, WASP's downstream partner in the signaling cascade.
IgA triggers immune responses by binding to Fc receptors on cells of the immune system. The structure of IgA1-Fc in a complex with two molecules of FcαRI provides clues that may explain the selectivity of IgA-mediated immune events.
The structure of the calcium-bound core of human cardiac troponin reveals distinct subdomains connected by flexible linkers, implying that domain reorientation motions within the complex trigger muscle contraction.