scholarly journals The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK)

2012 ◽  
Vol 22 (12) ◽  
pp. 3900-3904 ◽  
Author(s):  
Christopher W. Davies ◽  
Joseph Chaney ◽  
Gregory Korbel ◽  
Dagmar Ringe ◽  
Gregory A. Petsko ◽  
...  
Viruses ◽  
2017 ◽  
Vol 9 (7) ◽  
pp. 168 ◽  
Author(s):  
Meritxell Granell ◽  
Mikiyoshi Namura ◽  
Sara Alvira ◽  
Shuji Kanamaru ◽  
Mark van Raaij

Open Biology ◽  
2012 ◽  
Vol 2 (8) ◽  
pp. 120071 ◽  
Author(s):  
Ravi K. Nookala ◽  
Lars Langemeyer ◽  
Angela Pacitto ◽  
Bernardo Ochoa-Montaño ◽  
Jane C. Donaldson ◽  
...  

Mutations in the renal tumour suppressor protein, folliculin, lead to proliferative skin lesions, lung complications and renal cell carcinoma. Folliculin has been reported to interact with AMP-activated kinase, a key component of the mammalian target of rapamycin pathway. Most cancer-causing mutations lead to a carboxy-terminal truncation of folliculin, pointing to a functional importance of this domain in tumour suppression. We present here the crystal structure of folliculin carboxy-terminal domain and demonstrate that it is distantly related to differentially expressed in normal cells and neoplasia (DENN) domain proteins, a family of Rab guanine nucleotide exchange factors (GEFs). Using biochemical analysis, we show that folliculin has GEF activity, indicating that folliculin is probably a distantly related member of this class of Rab GEFs.


Author(s):  
Alexandr Bolgov ◽  
Svetlana Korban ◽  
Dmitrii Luzik ◽  
Vladimir Zhemkov ◽  
Meewhi Kim ◽  
...  

This study presents the crystal structure of the N-terminal SH3 (SH3N) domain of growth factor receptor-bound protein 2 (Grb2) at 2.5 Å resolution. Grb2 is a small (215-amino-acid) adaptor protein that is widely expressed and involved in signal transduction/cell communication. The crystal structure of full-length Grb2 has previously been reported (PDB entry 1gri). The structure of the isolated SH3N domain is consistent with the full-length structure. The structure of the isolated SH3N domain was solved at a higher resolution (2.5 Å compared with 3.1 Å for the previously deposited structure) and made it possible to resolve some of the loops that were missing in the full-length structure. In addition, interactions between the carboxy-terminal region of the SH3N domain and the Sos1-binding sites were observed in the structure of the isolated domain. Analysis of these interactions provided new information about the ligand-binding properties of the SH3N domain of Grb2.


PLoS ONE ◽  
2010 ◽  
Vol 5 (9) ◽  
pp. e12992 ◽  
Author(s):  
Azin Nezami ◽  
Florence Poy ◽  
Angela Toms ◽  
Wei Zheng ◽  
Michael J. Eck

FEBS Open Bio ◽  
2016 ◽  
Vol 6 (3) ◽  
pp. 168-178 ◽  
Author(s):  
Vladimir A. Zhemkov ◽  
Anna A. Kulminskaya ◽  
Ilya B. Bezprozvanny ◽  
Meewhi Kim

EMBO Reports ◽  
2008 ◽  
Vol 9 (7) ◽  
pp. 642-647 ◽  
Author(s):  
Likun Wang ◽  
Lei Wang ◽  
Stefano Vavassori ◽  
Shengjian Li ◽  
Huimin Ke ◽  
...  

1999 ◽  
Vol 13 (10) ◽  
pp. 1263-1275 ◽  
Author(s):  
H. E. Xu ◽  
M. A. Rould ◽  
W. Xu ◽  
J. A. Epstein ◽  
R. L. Maas ◽  
...  

1986 ◽  
Vol 64 (7) ◽  
pp. 1346-1349 ◽  
Author(s):  
Farid R. Ahmed ◽  
Francis M. F. Chen ◽  
N. Leo Benoiton

A side product accompanying the reaction of N-methoxycarbonyl-L-valine anhydride with an amino acid anion in aqueous dimethylformamide has been characterized by an X-ray analysis as N,N′-bismethoxycarbonyl-L-valyl-L-valine, C14H24N2O7. The crystals are orthorhombic, space group P212121, a = 14.581(2), b = 17.110(2), c = 6.970(1) Å, Z = 4. The structure was determined by the direct method, and refined by block-diagonal least squares to R = 0.046, Rw = 0.053 for 1759 reflections with I ≥ 3σ(i). The carboxy-terminal part of the dimer is in the gauche conformation while the other part is trans. Each molecule at (x, y, z) makes two hydrogen bonds O … H—O and N—H … O to the molecule at (1 − x, y − 1/2, 1/2 − z) and similarly to that at (1 − x, 1/2 + y, 1/2 − z) to form infinite ribbons along y.


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