Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs. [PDF]
Protein Sci, 2014 AbstractThe FK506‐binding protein (FKBP) family consists of proteins with a variety of protein–protein interaction domains and versatile cellular functions. It is assumed that all members are peptidyl‐prolyl cis–trans isomerases with the enzymatic function attributed to the FKBP domain.
Boudko SP +4 more
europepmc +5 more sources
The number and location of EF hand motifs dictates the calcium dependence of polycystin-2 function.
FASEB J, 2014 ABSTRACT Polycystin 2 (PC2) is a calcium‐dependent calcium channel, and mutations to human PC2 (hPC2) are associated with polycystic kidney disease. The C‐terminal tail of hPC2 contains 2 EF hand motifs, but only the second binds calcium.
Kuo IY +6 more
europepmc +5 more sources
Interleukin-11 binds specific EF-hand proteins via their conserved structural motifs
Journal of Biomolecular Structure and Dynamics, 2017 Interleukin-11 (IL-11) is a hematopoietic cytokine engaged in numerous biological processes and validated as a target for treatment of various cancers. IL-11 contains intrinsically disordered regions that might recognize multiple targets.
A. S. Kazakov +16 more
semanticscholar +5 more sources
Genus-Wide Pan-Genome Analysis of Oryza Calcium-Dependent Protein Kinase Genes and Their Related Kinases Highlights the Complexity of Protein Domain Architectures and Expression Dynamics [PDF]
PlantsThe Oryza genus serves not only as a gene pool for rice improvement but also as a model system for plant evolutionary research. Calcium-dependent protein kinases (CPKs) function as both effectors and sensors in calcium signaling and play versatile roles ...
Fu Shi +7 more
doaj +2 more sources
A Deep Dive into the N-Terminus of STIM Proteins: Structure–Function Analysis and Evolutionary Significance of the Functional Domains [PDF]
BiomoleculesCalcium is an important second messenger that is involved in almost all cellular processes. Disruptions in the regulation of intracellular Ca2+ levels ([Ca2+]i) adversely impact normal physiological function and can contribute to various diseased ...
Sasirekha Narayanasamy +2 more
doaj +2 more sources
EF‐hand motifs in inositol phospholipid‐specific phospholipase C [PDF]
FEBS Letters, 1990 Computer sequence analysis with a linear weight matrix revealed the presence of one canonical EF‐hand motif in the δ isoform of inositol phospholipid‐specific phospholipase C and one ancestral EF‐hand in the γ form.
A. Bairoch, J. Cox
semanticscholar +4 more sources
A Calcium-binding Protein with Four EF-hand Motifs in Streptomyces ambofaciens
Bioscience, Biotechnology, and Biochemistry, 2001 A gene (cabA) encoding a calcium-binding protein was cloned from Streptomyces ambofaciens. CabA was 180 amino acid residues long and contained four typical EF-hand motifs bearing high sequence similarity to the calcium-binding sites in calmodulin. Consistent with this, CabA showed distinct calcium-binding activity, comparable to bovine brain calmodulin.
T. Yonekawa, Y. Ohnishi, S. Horinouchi
semanticscholar +3 more sources
A growing family of the Ca2+-binding proteins with five EF-hand motifs.
Biochemical Journal, 1997 M. Maki, S. Narayana, K. Hitomi
semanticscholar +2 more sources
Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins
Biomolecules, 2021 Motifs within proteins help us categorize their functions. Intrinsically disordered proteins (IDPs) are rich in short linear motifs, conferring them many different roles.
Estella A. Newcombe +7 more
doaj +1 more source
PLoS ONE, 2021 Calmodulin, a ubiquitous eukaryotic calcium sensor responsible for the regulation of many fundamental cellular processes, is a highly flexible protein and exhibits an unusually wide range of conformations.
Shivani Yaduvanshi +2 more
doaj +1 more source