A Divalent Metal Ion Binding Site in the Kinase Insert Domain of the .alpha.-Platelet-Derived Growth Factor Receptor Regulates Its Association with SH2 Domains

Biochemistry ◽  
1995 ◽  
Vol 34 (7) ◽  
pp. 2095-2106 ◽  
Author(s):  
Daruka Mahadevan ◽  
Narmada Thanki ◽  
Pilar Aroca ◽  
Peter McPhie ◽  
Jin-Chen Yu ◽  
...  
Keyword(s):  
Growth Factor ◽  
Binding Site ◽  
Metal Ion ◽  
Growth Factor Receptor ◽  
Divalent Metal ◽  
Platelet Derived Growth Factor ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Sh2 Domains ◽  
Divalent Metal Ion

H101G Mutation in Rat Lens αB-Crystallin Alters Chaperone Activity and Divalent Metal Ion Binding

2021 ◽  
Vol 22 ◽  
Author(s):  
Yi-Ying Wu ◽  
Naveen Kumar Reddy Desu ◽  
Shou-Yun Lu ◽  
Bi-Yu Yu ◽  
Ramya Kumar ◽  
...  
Keyword(s):  
Binding Site ◽  
Metal Ion ◽  
Divalent Metal ◽  
Chaperone Activity ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Functional Changes ◽  
Αb Crystallin ◽  
Divalent Metal Ion ◽  
The Stability

Background: The molecular chaperone function of αB-crystallins is heavily involved in maintaining lens transparency and the development of cataracts. Objective: To study whether divalent metal ion binding improves the stability and αB-crystallin chaperone activity. Results: Substitution of His101 with glycine resulted in structural and functional changes. Spectral analysis and chaperone-like activity assays showed that substitution of glycine resulted in a higher percentage of random coils, increased hydrophobicity, and 22±2% higher chaperone-like activity. Whereas in the presence of the Cu2+ ion, H101G exhibited 32±1% less chaperone-like activity compared to the wild type. Conclusion: Cu2+ has been reported to enhance the chaperone-like activity of lens α-crystallin. Our results indicate that H101 is the predominant Cu2binding site, and the mutation resulted in a partial unfolding that impaired the binding of Cu2+ to H101 residue. In conclusion, this study further helps to understand the important binding site for Cu2+ to αB-crystallin.

scholarly journals Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme

RNA ◽  
2000 ◽  
Vol 6 (4) ◽  
pp. 511-519 ◽  
Author(s):  
ERIC L. CHRISTIAN ◽  
NICHOLAS M. KAYE ◽  
MICHAEL E. HARRIS
Keyword(s):  
Binding Site ◽  
Metal Ion ◽  
Divalent Metal ◽  
Ribonuclease P ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Divalent Metal Ion ◽  
Conserved Core

His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms

2014 ◽  
Vol 19 (7) ◽  
pp. 1149-1164 ◽  
Author(s):  
Mireia Tomas ◽  
María Ayelen Pagani ◽  
Carlos S. Andreo ◽  
Mercè Capdevila ◽  
Roger Bofill ◽  
...  
Keyword(s):  
Comparative Study ◽  
Metal Ion ◽  
Divalent Metal ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Divalent Metal Ion

IR-Spectroscopic and Theoretical Studies of the Divalent Metal Ion Binding To DNA

1997 ◽  
pp. 387-388
Author(s):  
V. V. Andrushchenko ◽  
S. V. Kornilova ◽  
L. E. Kapinos ◽  
E. V. Hackl ◽  
Yu P. Blagoi
Keyword(s):  
Metal Ion ◽  
Divalent Metal ◽  
Ion Binding ◽  
Theoretical Studies ◽  
Metal Ion Binding ◽  
Divalent Metal Ion ◽  
Ir Spectroscopic
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