Calcium-Binding Proteins of the EF-Hand Superfamily

2019 ◽  
Keyword(s):  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Ef Hand

scholarly journals Comparison of terbium (III) luminescence enhancement in mutants of EF hand calcium binding proteins.

1992 ◽  
Vol 267 (19) ◽  
pp. 13340-13347
Author(s):  
C.W. Hogue ◽  
J.P. MacManus ◽  
D Banville ◽  
A.G. Szabo
Keyword(s):  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Luminescence Enhancement ◽  
Ef Hand

scholarly journals S100A14, a Member of the EF-hand Calcium-binding Proteins, Is Overexpressed in Breast Cancer and Acts as a Modulator of HER2 Signaling

2013 ◽  
Vol 289 (2) ◽  
pp. 827-837 ◽  
Author(s):  
Chengshan Xu ◽  
Hongyan Chen ◽  
Xiang Wang ◽  
Jidong Gao ◽  
Yiqun Che ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Ef Hand ◽  
Her2 Signaling

A change-in-hand mechanism for S100 signalling

1998 ◽  
Vol 76 (2-3) ◽  
pp. 324-333 ◽  
Author(s):  
Steven P Smith ◽  
Gary S Shaw
Keyword(s):  
Conformational Change ◽  
Calcium Ion ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Three Dimensional ◽  
Calcium Binding Proteins ◽  
C Terminus ◽  
Ef Hand ◽  
Sensor Proteins ◽  
Binding Loop

S100 proteins are a group of small dimeric calcium-binding proteins making up a large subclass of the EF-hand family of calcium-binding proteins. Members of this family of proteins have been proposed to act as intracellular calcium modulatory proteins in a fashion analogous to that of the EF-hand sensor proteins troponin-C and calmodulin. Recently, NMR spectroscopy has provided the three-dimensional structures of the S100 family members S100A6 and S100B in both the apo- and calcium-bound forms. These structures have allowed for the identification of a novel calcium-induced conformational change termed the change-in-hand mechanism. Helix III of the C-terminal calcium-binding loop changes its helix-helix interactions (or handness) with the remainder of the molecule primarily owing to the reorientation of the backbone in an effort to coordinate the calcium ion. This reorientation of helix III exposes several residues in the C-terminus and linker regions of S100B resulting in the formation of a hydrophobic patch surrounded be a number of acidic residues. This site is the proposed region for protein-protein recognition.Key words: S100, calcium-binding protein, EF-hand, conformational change.

scholarly journals The gene family of EF-hand calcium-binding proteins from the flagellum of Trypanosoma brucei

1994 ◽  
Vol 304 (3) ◽  
pp. 833-841 ◽  
Author(s):  
Y Wu ◽  
J Deford ◽  
R Benjamin ◽  
M G Lee ◽  
L Ruben
Keyword(s):  
Amino Acid ◽  
Trypanosoma Brucei ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Direct Repeat ◽  
Calcium Binding Proteins ◽  
Amino Acid Sequences ◽  
Reading Frame ◽  
Genomic Clones ◽  
Ef Hand

The flagellum of Trypanosoma brucei contains calmodulin, and a separate family of antigenically related EF-hand calcium-binding proteins which we call calflagins. The following study evaluates the structure and genomic organization of the calflagin family. Genomic Southern blots indicated that multiple copies of calflagin genes occurred in T. brucei, and that all of these copies were contained in a single 23 kb XhoI-XhoI fragment on chromosomes 15 and 16 mRNAs of 1.2 and 1.6 kb were identified in bloodstream and procyclic life-cycle stages. Genomic fragments of 2.5 and 1.7 kb were cloned that encoded calflagin sequences. The calflagin genes were arranged tandemly along the genomic fragments. Three new members of the calflagin family were sequenced from a cDNA clone and the two genomic clones. Two unrelated families of 3′ flanking sequences were downstream from the calflagin genes. An open reading frame that was unrelated to any calflagin sequence was at the 5′ end of the 2.5 kb genomic fragment. The deduced amino acid sequences of the genomic clones (called Tb-24 and Tb-1.7g) were similar to the previously described Tb-17. Each encoded an approximately 24 kDa protein which contained three EF-hand calcium-binding motifs and one degenerate EF-hand motif. The cDNA encoded a protein (called Tb-44A) which was approximately twice as large as the other calflagins. The large size resulted from a nearly direct repeat of 186 amino acids. In general, variability among the T. brucei calflagins was greater than observed for related proteins from Trypanosoma cruzi. We demonstrate that this variability resulted from amino acid substitutions at the N-terminus, C-terminal extensions, and duplication of internal segments.

scholarly journals Calciomics: prediction and analysis of EF-hand calcium binding proteins by protein engineering

2010 ◽  
Vol 53 (1) ◽  
pp. 52-60 ◽  
Author(s):  
YanYi Chen ◽  
ShengHui Xue ◽  
YuBin Zhou ◽  
Jenny Jie Yang
Keyword(s):  
Protein Engineering ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Ef Hand

scholarly journals Endonuclease-like activity of the N-terminal domain of Euplotes octocarinatus centrin

RSC Advances ◽  
2017 ◽  
Vol 7 (82) ◽  
pp. 51773-51788 ◽  
Author(s):  
Wenlong Zhang ◽  
Enxian Shi ◽  
Yanan Feng ◽  
Yaqin Zhao ◽  
Binsheng Yang
Keyword(s):  
Nucleotide Excision Repair ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Excision Repair ◽  
Calcium Binding Proteins ◽  
Terminal Domain ◽  
Nucleotide Excision ◽  
Ef Hand ◽  
Euplotes Octocarinatus

Euplotes octocarinatus centrin (EoCen) is a member of the EF-hand superfamily of calcium-binding proteins, which refer to nucleotide excision repair (NER).

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