scholarly journals A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition.

1992 ◽  
Vol 89 (6) ◽  
pp. 2032-2035 ◽  
Author(s):  
W. T. Miller ◽  
P. Schimmel
Keyword(s):  
Metal Binding ◽  
Trna Synthetase ◽  
Binding Motif ◽  
Aminoacyl Trna Synthetase ◽  
Trna Recognition ◽  
Metal Binding Motif

scholarly journals Metal Binding Motif in the Active Site of the HDV Ribozyme Binds Divalent and Monovalent Ions

Biochemistry ◽  
2011 ◽  
Vol 50 (13) ◽  
pp. 2672-2682 ◽  
Author(s):  
Narayanan Veeraraghavan ◽  
Abir Ganguly ◽  
Jui-Hui Chen ◽  
Philip C. Bevilacqua ◽  
Sharon Hammes-Schiffer ◽  
...  
Keyword(s):  
Active Site ◽  
Metal Binding ◽  
Binding Motif ◽  
Monovalent Ions ◽  
Hdv Ribozyme ◽  
Metal Binding Motif

scholarly journals Metal ion recognition of the metal-binding motif in hammerhead ribozymes

2003 ◽  
Vol 43 (supplement) ◽  
pp. S28
Author(s):  
Y. Tanaka ◽  
Y. Kasai ◽  
C. Kojima ◽  
K. Yamasaki ◽  
H. Morita ◽  
...  
Keyword(s):  
Metal Binding ◽  
Metal Ion ◽  
Binding Motif ◽  
Hammerhead Ribozymes ◽  
Ion Recognition ◽  
Metal Binding Motif

scholarly journals Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization

2004 ◽  
Vol 166 (7) ◽  
pp. 1003-1014 ◽  
Author(s):  
Gideon Lansbergen ◽  
Yulia Komarova ◽  
Mauro Modesti ◽  
Claire Wyman ◽  
Casper C. Hoogenraad ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Metal Binding ◽  
Intramolecular Interaction ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Scanning Force Microscopy ◽  
Binding Motif ◽  
Force Microscopy ◽  
Scanning Force ◽  
Metal Binding Motif

Cytoplasmic linker protein (CLIP)-170, CLIP-115, and the dynactin subunit p150Glued are structurally related proteins, which associate specifically with the ends of growing microtubules (MTs). Here, we show that down-regulation of CLIP-170 by RNA interference results in a strongly reduced accumulation of dynactin at the MT tips. The NH2 terminus of p150Glued binds directly to the COOH terminus of CLIP-170 through its second metal-binding motif. p150Glued and LIS1, a dynein-associating protein, compete for the interaction with the CLIP-170 COOH terminus, suggesting that LIS1 can act to release dynactin from the MT tips. We also show that the NH2-terminal part of CLIP-170 itself associates with the CLIP-170 COOH terminus through its first metal-binding motif. By using scanning force microscopy and fluorescence resonance energy transfer-based experiments we provide evidence for an intramolecular interaction between the NH2 and COOH termini of CLIP-170. This interaction interferes with the binding of the CLIP-170 to MTs. We propose that conformational changes in CLIP-170 are important for binding to dynactin, LIS1, and the MT tips.

The metal-binding motif of dipeptidyl peptidase III directly influences the enzyme activity in the copper derivative of dipeptidyl peptidase III

2004 ◽  
Vol 431 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Junzo Hirose ◽  
Hiroshi Kamigakiuchi ◽  
Hiroyuki Iwamoto ◽  
Hideaki Fujii ◽  
Masanori Nakai ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Metal Binding ◽  
Dipeptidyl Peptidase ◽  
Binding Motif ◽  
Metal Binding Motif

scholarly journals Interaction between a metal-binding motif of Hammerhead Ribozyme and divalent cations

2000 ◽  
Vol 40 (supplement) ◽  
pp. S94
Author(s):  
Y. Tanaka ◽  
E.H. Morita ◽  
H. Hayashi ◽  
Y. Kasa ◽  
T. Tanaka ◽  
...  
Keyword(s):  
Metal Binding ◽  
Divalent Cations ◽  
Hammerhead Ribozyme ◽  
Binding Motif ◽  
Metal Binding Motif

Embedding a Metal-Binding Motif for Copper Transporter into a Lipid Bilayer by Cu(I) Binding

2018 ◽  
Vol 122 (24) ◽  
pp. 6364-6370 ◽  
Author(s):  
Mariko Okada ◽  
Shinji Kajimoto ◽  
Takakazu Nakabayashi
Keyword(s):  
Lipid Bilayer ◽  
Metal Binding ◽  
Binding Motif ◽  
Copper Transporter ◽  
Metal Binding Motif
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