scholarly journals Huntingtin: A Protein with a Peculiar Solvent Accessible Surface

2021 ◽  
Vol 22 (6) ◽  
pp. 2878
Author(s):  
Giulia Babbi ◽  
Castrense Savojardo ◽  
Pier Luigi Martelli ◽  
Rita Casadio
Keyword(s):  
Electron Microscopy ◽  
Physicochemical Properties ◽  
Computational Methods ◽  
Binding Sites ◽  
Calcium Binding ◽  
Functional Annotation ◽  
Present Knowledge ◽  
Calcium Binding Sites ◽  
Accessible Surface ◽  
Solvent Accessible Surface

Taking advantage of the last cryogenic electron microscopy structure of human huntingtin, we explored with computational methods its physicochemical properties, focusing on the solvent accessible surface of the protein and highlighting a quite interesting mix of hydrophobic and hydrophilic patterns, with the prevalence of the latter ones. We then evaluated the probability of exposed residues to be in contact with other proteins, discovering that they tend to cluster in specific regions of the protein. We then found that the remaining portions of the protein surface can contain calcium-binding sites that we propose here as putative mediators for the protein to interact with membranes. Our findings are justified in relation to the present knowledge of huntingtin functional annotation.

scholarly journals Mutation of the high affinity calcium binding sites in cardiac troponin C.

1992 ◽  
Vol 267 (2) ◽  
pp. 825-831 ◽  
Author(s):  
J C Negele ◽  
D G Dotson ◽  
W Liu ◽  
H L Sweeney ◽  
J A Putkey
Keyword(s):  
Binding Sites ◽  
Calcium Binding ◽  
Cardiac Troponin ◽  
Troponin C ◽  
High Affinity ◽  
Cardiac Troponin C ◽  
Calcium Binding Sites

Rat GTP cyclohydrolase I is a homodecameric protein complex containing high-affinity calcium-binding sites 1 1Edited by W. Baumeister

1998 ◽  
Vol 279 (1) ◽  
pp. 189-199 ◽  
Author(s):  
Michel O Steinmetz ◽  
Christoph Plüss ◽  
Urs Christen ◽  
Bettina Wolpensinger ◽  
Ariel Lustig ◽  
...  
Keyword(s):  
Protein Complex ◽  
Binding Sites ◽  
Calcium Binding ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase ◽  
High Affinity ◽  
Calcium Binding Sites

scholarly journals Characterization of the calcium-binding sites of calcineurin B

FEBS Letters ◽  
1995 ◽  
Vol 362 (1) ◽  
pp. 55-58 ◽  
Author(s):  
Lazaros T Kakalis ◽  
Michael Kennedy ◽  
Robert Sikkink ◽  
Frank Rusnak ◽  
Ian M Armitage
Keyword(s):  
Binding Sites ◽  
Calcium Binding ◽  
Calcineurin B ◽  
Calcium Binding Sites

scholarly journals Conformational epitopes at cadherin calcium-binding sites and p120-catenin phosphorylation regulate cell adhesion

2012 ◽  
Vol 23 (11) ◽  
pp. 2092-2108 ◽  
Author(s):  
Yuliya I. Petrova ◽  
MarthaJoy M. Spano ◽  
Barry M. Gumbiner
Keyword(s):  
Cell Surface ◽  
Conformational Changes ◽  
Binding Sites ◽  
Calcium Binding ◽  
Cell Types ◽  
P120 Catenin ◽  
Physiological Regulation ◽  
Conformational Epitopes ◽  
Calcium Binding Sites ◽  
E Cadherin

We investigated changes in cadherin structure at the cell surface that regulate its adhesive activity. Colo 205 cells are nonadhesive cells with a full but inactive complement of E-cadherin–catenin complexes at the cell surface, but they can be triggered to adhere and form monolayers. We were able to distinguish the inactive and active states of E-cadherin at the cell surface by using a special set of monoclonal antibodies (mAbs). Another set of mAbs binds E-cadherin and strongly activates adhesion. In other epithelial cell types these activating mAbs inhibit growth factor–induced down-regulation of adhesion and epithelial morphogenesis, indicating that these phenomena are also controlled by E-cadherin activity at the cell surface. Both types of mAbs recognize conformational epitopes at different interfaces between extracellular cadherin repeat domains (ECs), especially near calcium-binding sites. Activation also induces p120-catenin dephosphorylation, as well as changes in the cadherin cytoplasmic domain. Moreover, phospho-site mutations indicate that dephosphorylation of specific Ser/Thr residues in the N-terminal domain of p120-catenin mediate adhesion activation. Thus physiological regulation of the adhesive state of E-cadherin involves physical and/or conformational changes in the EC interface regions of the ectodomain at the cell surface that are mediated by catenin-associated changes across the membrane.

Calcium-Binding Sites of Calmodulin and Electron Transfer by Inducible Nitric Oxide Synthase†

Biochemistry ◽  
2005 ◽  
Vol 44 (20) ◽  
pp. 7593-7601 ◽  
Author(s):  
Irena Gribovskaja ◽  
Kaleb C. Brownlow ◽  
Sam J. Dennis ◽  
Andrew J. Rosko ◽  
Michael A. Marletta ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Electron Transfer ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Binding Sites ◽  
Calcium Binding ◽  
Calcium Binding Sites ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

scholarly journals Functional Roles of the Non-Catalytic Calcium-Binding Sites in the N-Terminal Domain of Human Peptidylarginine Deiminase 4

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e51660 ◽  
Author(s):  
Yi-Liang Liu ◽  
I-Chen Tsai ◽  
Chia-Wei Chang ◽  
Ya-Fan Liao ◽  
Guang-Yaw Liu ◽  
...  
Keyword(s):  
Binding Sites ◽  
Calcium Binding ◽  
Peptidylarginine Deiminase ◽  
Functional Roles ◽  
Peptidylarginine Deiminase 4 ◽  
Terminal Domain ◽  
Calcium Binding Sites
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