ArticleProtein science : a publication of the Protein Society2014
Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Biophysical characterization of Cyclophilin B reveals membrane localization as its primary functional determinant as a prolyl isomerase.Protein science : a publication of the Protein Society · 2026Article
- The stability of FKBP9 maintained by BiP is crucial for glioma progression.Genes & diseases · 2024Article
- Local Net Charge State of Collagen Triple Helix Is a Determinant of FKBP22 Binding to Collagen III.International journal of molecular sciences · 2023Article
- Identification, characterization and spatiotemporal expression analysis of the FKBP family genes in Locusta migratoria.Scientific reports · 2023Article
- Genome-wide characterization of FK506-binding proteins, parvulins and phospho-tyrosyl phosphatase activators in wheat and their regulation by heat stress.Frontiers in plant science · 2022Article
- The Ehlers-Danlos syndromes.Nature reviews. Disease primers · 2020Review
- Article
- Comparative analysis of FKBP family protein: evaluation, structure, and function in mammals and Drosophila melanogaster.BMC developmental biology · 2018Review
- A cohort of 17 patients with kyphoscoliotic Ehlers-Danlos syndrome caused by biallelic mutations in FKBP14: expansion of the clinical and mutational spectrum and description of the natural history.Genetics in medicine : official journal of the American College of Medical Genetics · 2018Article
- Ziploc-ing the structure 2.0: Endoplasmic reticulum-resident peptidyl prolyl isomerases show different activities toward hydroxyproline.The Journal of biological chemistry · 2017Article
- Golgi enzymes do not cycle through the endoplasmic reticulum during protein secretion or mitosis.Molecular biology of the cell · 2017Article
- The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease.Molecular neurobiology · 2016Review
- FK506-Binding Proteins and Their Diverse Functions.Current molecular pharmacology · 2015Review
- A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis.The Journal of biological chemistry · 2014Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 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. Six members of this family localize to the mammalian endoplasmic reticulum (ER). Four of them, FKBP22 (encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65 (FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. Little is known about the biological roles of these proteins, but emerging genetics studies are attracting great interest to the ER resident FKBPs, as mutations in genes encoding FKBP10 and FKBP14 were shown to cause a variety of matrix disorders. Although the structural organization of the FKBP-type domain as well as of the EF-hand motif has been known for a while, it is difficult to conclude how these structures are combined and how it affects the protein functionality. We have determined a unique 1.9 Å resolution crystal structure for human FKBP22, which can serve as a prototype for other EF hand-containing FKBPs. The EF-hand motifs of two FKBP22 molecules form a dimeric complex with an elongated and predominantly hydrophobic cavity that can potentially be occupied by an aliphatic ligand. The FKBP-type domains are separated by a cleft and their putative active sites can catalyze isomerazation of two bonds within a polypeptide chain in extended conformation. These structural results are of prime interest for understanding biological functions of ER resident FKBPs containing EF-hand motifs.
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