Designed leucine‐rich repeat proteins bind two muramyl dipeptide ligands

2021 ◽  
Author(s):  
Christina S. Kim ◽  
Anne M. Brown ◽  
Tijana Z. Grove ◽  
Felicia A. Etzkorn

2016 ◽  
Vol 16 (5) ◽  
pp. 400-414 ◽  
Author(s):  
Nora Hermes ◽  
Stefanie Kewitz ◽  
Martin S. Staege


1996 ◽  
Vol 35 (1-2) ◽  
pp. 31-40 ◽  
Author(s):  
Akihiko Taguchi ◽  
Akio Wanaka ◽  
Tetsuji Mori ◽  
Kazumasa Matsumoto ◽  
Yuji Imai ◽  
...  


2002 ◽  
Vol 42 (supplement2) ◽  
pp. S93
Author(s):  
P Enhkbayar ◽  
M. Oosaki ◽  
Masakatsu M. ◽  
N. Matsushima


2010 ◽  
Vol 286 (7) ◽  
pp. 5727-5735 ◽  
Author(s):  
Kyoung-Hee Lee ◽  
Yuen-Joyce Liu ◽  
Amlan Biswas ◽  
Chikako Ogawa ◽  
Koichi S. Kobayashi


1994 ◽  
Vol 19 ◽  
pp. S124
Author(s):  
Akihiko Taguchi ◽  
Akio Wanaka ◽  
Tetsuji Mori ◽  
Kazumasa Matsumoto ◽  
Yuji Imai ◽  
...  


2002 ◽  
Vol 103 (s47) ◽  
pp. 67P.3-68P
Author(s):  
LC Andreae ◽  
J. Gilthorpe ◽  
A Lumsden


Cell ◽  
1996 ◽  
Vol 84 (3) ◽  
pp. 451-459 ◽  
Author(s):  
Mark S Dixon ◽  
David A Jones ◽  
James S Keddie ◽  
Colwyn M Thomas ◽  
Kate Harrison ◽  
...  




2007 ◽  
Vol 02 (03n04) ◽  
pp. 207-219 ◽  
Author(s):  
ANSUMAN LAHIRI ◽  
SOUMALEE BASU

We have studied the collective dynamics of leucine-rich repeat (LRR) proteins using an elastic network approximation. The slowest mode of the porcine ribonuclease inhibitor (pRI) protein could be visualized as bending fluctuations of a curved elastic strip leading to a planar opening–closing motion of the horseshoe which largely corresponded to the deformation of the protein on ligand binding. The second slowest mode however exhibited a significant out of plane splaying. The distribution of the lowest eigenvalues of different LRR proteins as a function of their repeat number was found to be close to the dispersion curve obtained from pRI whereas that of the leucine-rich variant (LRV) protein showed considerable deviation. The differing mechanical properties of these structurally similar solenoid proteins may have relevance to their function.



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