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Engineering Strontium Binding Affinity in an EF-hand Motif: A Quantum Chemical and Molecular Dynamics Study

Journal of Biomolecular Structure and Dynamics, 2004
Proteins with the ability to specifically bind strontium would potentially be of great use in the field of nuclear waste management. Unfortunately, no such peptides or proteins are known -- indeed, it is uncertain whether they exist under natural conditions due to low environmental concentrations of strontium. To investigate the possibility of devising
D, Rinaldo, C, Vita, M J, Field
openaire   +2 more sources

Probing Ca2+-Binding Capability of Viral Proteins with the EF-Hand Motif by Grafting Approach

2012
Ca(2+) is implicated in almost every step of the life cycle of viruses, including virus entry into host cells, virus replication, virion assembly, maturation, and release. However, due to the lack of prediction algorithms and rigorous validation methods, only limited cases of viral Ca(2+)-binding sites are reported.
Yubin, Zhou   +3 more
openaire   +2 more sources

A unique EF-hand motif in mnemiopsin photoprotein from Mnemiopsis leidyi: Implication for its low calcium sensitivity

Biochemical and Biophysical Research Communications, 2011
Up to now, all reported Ca(2+)-regulated photoproteins, except for mnemiopsin, have been cloned and expressed in Escherichia coli. In this study, the cDNA for an isotype of mnemiopsin, from the ctenophore Mnemiopsis leidyi, has been cloned, sequenced, and functionally expressed. The full length cDNA encoding mnemiopsin of M.
Vahab, Jafarian   +6 more
openaire   +2 more sources

Sequence motifs determine structure and Ca++-binding by EF-hand proteins.

Journal of molecular microbiology and biotechnology, 2000
Prediction of protein structural and functional characteristics based on specific motif interactions could serve as a powerful tool in many facets of the biological sciences. Such improvements in protein modeling will be instrumental in the enhancement of drug design. A new approach to a sequence description of EF-hand motifs with more than one EF-hand
H H, Rashidi   +3 more
openaire   +1 more source

Expression and characterization of EF-hand I loop mutants of aequorin replaced with other loop sequences of Ca2+-binding proteins: an approach to studying the EF-hand motif of proteins

Journal of Biochemistry, 2016
The binding properties of Ca(2+) to EF-hand I of aequorin (AQ) were characterized by replacing the loop sequence of EF-hand I (AQ[I]) with other known loop sequences of Ca(2+)-binding proteins, including photoproteins (aequorin, clytin-I, clytin-II and mitrocomin), Renilla luciferin-binding protein (RLBP) and calmodulin (CaM).
Satoshi, Inouye, Yuiko, Sahara-Miura
openaire   +2 more sources

Cloning of a 21.7-kDa vaccine-dominant antigen gene of Schistosoma mansoni reveals an EF hand-like motif

Molecular and Biochemical Parasitology, 1992
Several cDNA clones encoding a 21.7-kDa antigen (Sm21.7) were detected from a Schistosoma mansoni sporocyst cDNA expression library using irradiated cercaria-vaccinated rabbit serum. The antigen was designated 'vaccine dominant' because parasite-derived Sm21.7 was recognised preferentially by mouse vaccine sera compared with mouse infection sera.
P, Francis, Q, Bickle
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Characterization of Rab45/RASEF containing EF-hand domain and a coiled-coil motif as a self-associating GTPase

Biochemical and Biophysical Research Communications, 2007
Rab-family GTPases function as key regulators for membrane traffic. Among them, Rab45/RASEF is an atypical GTPase in that it contains a coiled-coil motif at the mid region and a distinct N-terminal EF-hand domain with C-terminal Rab-homology domain. Here, we provide the initial biochemical characterization and intracellular localization of human Rab45.
Mami, Shintani   +5 more
openaire   +2 more sources

Liaison between Myristoylation and Cryptic EF-Hand Motif Confers Ca2+Sensitivity to Neuronal Calcium Sensor-1

Biochemistry, 2015
Many members of the neuronal calcium sensor (NCS) protein family have a striking coexistence of two characteristics, that is, N-myristoylation and the cryptic EF-1 motif. We investigated the rationale behind this correlation in neuronal calcium sensor-1 (NCS-1) by restoring Ca(2+) binding ability of the disabled EF-1 loop by appropriate mutations.
Vangipurapu, Rajanikanth   +5 more
openaire   +2 more sources

Functional dissection of DNA supercoiling factor: EF‐hand domains and C‐terminal HDEF motif are essential for its activity

Genes to Cells, 1999
DNA supercoiling factor (SCF) was first identified in the silkworm as a protein capable of generating negative supercoils into a relaxed DNA in conjunction with eukaryotic topoisomerase II. Drosophila melanogaster SCF localizes to puffs on polytene chromosomes, implicating its role in gene expression.
M, Kobayashi, S, Hirose
openaire   +2 more sources

Tuning the Equilibrium Ion Affinity and Selectivity of the EF-Hand Calcium Binding Motif:  Substitutions at the Gateway Position

Biochemistry, 1996
The ion binding parameters of the EF-hand Ca2+ binding motif are carefully tuned for different biological applications. The present study examines the contribution of the ninth position of the Ca2+-coordinating EF-loop to the tuning of Ca2+ affinity and selectivity, using the model EF-loop of the Escherichia coli galactose binding protein.
S K, Drake, K L, Lee, J J, Falke
openaire   +2 more sources

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