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The Crystal Structure of JNK2 Reveals Conformational Flexibility in the MAP Kinase Insert and Indicates Its Involvement in the Regulation of Catalytic Activity

✍ Scribed by David Shaw; Sandra M. Wang; Armando G. Villaseñor; Stan Tsing; David Walter; Michelle F. Browner; Jim Barnett; Andreas Kuglstatter


Book ID
116663887
Publisher
Elsevier Science
Year
2008
Tongue
English
Weight
912 KB
Volume
383
Category
Article
ISSN
0022-2836

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High resolution crystal structures of tr
✍ Rajaram Venkatesan; Markus Alahuhta; Petri M. Pihko; Rik K. Wierenga 📂 Article 📅 2011 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 720 KB

## Abstract The key residue of the active site of triosephosphate isomerase (TIM) is the catalytic glutamate, which is proposed to be important (i) as a catalytic base, for initiating the reaction, as well as (ii) for the subsequent proton shuttling steps. The structural properties of this glutamat