Back Cover: Visualizing an Ultra‐Weak Protein–Protein Interaction in Phosphorylation Signaling (Angew. Chem. Int. Ed. 43/2014). Issue 43 (14th August 2014)

• Record Type: Journal Article
• Authors: Xing, Qiong; Huang, Peng; Yang, Ju; Sun, Jian‐Qiang; Gong, Zhou; Dong, Xu; Guo, Da‐Chuan; Chen, Shao‐Min; Yang, Yu‐Hong; Wang, Yan; Yang, Ming‐Hui; Yi, Ming; Ding, Yi‐Ming; Liu, Mai‐Li; Zhang, Wei‐Ping; Tang, Chun
• Is Part Of: Angewandte Chemie international edition. Volume 53:Issue 43(2014)
• Page Start: 11666
• Page End: 11666
• Publication Date: 2014-08-14
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201407928
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Proteins interact …︁</bold> in a transient yet specific manner to relay signals within the crowded cellular environment. In their Communication on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">page 11501 ff., </ext-link> C. Tang, W.‐P. Zhang, and co‐workers show that phosphorylation signaling can take place between two proteins with a binding affinity of only 25 m<sc>M</sc> and a complex lifetime in the μs–ms range, which is an order of magnitude weaker than all known protein–protein interactions. Such ultra‐weak and fleeting interactions could be prevalent among signaling proteins.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgh2cgjt87q" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>