ArticleProceedings of the National Academy of Sciences of the United States of America1996
Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 108 citations in OpenAlex.
- The nucleocytoplasmic translocation of HINT1 regulates the maturation of cell density.Life science alliance · 2025Article
- Human HINT1 Mutant Proteins that Cause Axonal Motor Neuropathy Exhibit Anomalous Interactions with Partner Proteins.Molecular neurobiology · 2021Article
- Comparative Proteomic Study Shows the Expression of Hint-1 in Pituitary Adenomas.Diagnostics (Basel, Switzerland) · 2021Article
- The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and Calmodulin-Regulated Cysteine SUMO Protease.Antioxidants & redox signaling · 2019Article
- Crystal Structure of Histidine Triad Nucleotide-Binding Protein from the Pathogenic FungusMolecules and cells · 2019Article
- Altered Light Conditions Contribute to Abnormalities in Emotion and Cognition Through HINT1 Dysfunction in C57BL/6 Mice.Frontiers in behavioral neuroscience · 2018Article
- Errors in Crystal structure of HINT from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Crystal structure of HINT from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Structures of a histidine triad family protein from Entamoeba histolytica bound to sulfate, AMP and GMP.Acta crystallographica. Section F, Structural biology communications · 2015Article
- The σ1 receptor engages the redox-regulated HINT1 protein to bring opioid analgesia under NMDA receptor negative control.Antioxidants & redox signaling · 2015Article
- Specific non-local interactions are not necessary for recovering native protein dynamics.PloS one · 2014Article
- Nitric oxide and zinc-mediated protein assemblies involved in mu opioid receptor signaling.Molecular neurobiology · 2013Review
- HINT1 protein cooperates with cannabinoid 1 receptor to negatively regulate glutamate NMDA receptor activity.Molecular brain · 2013Article
- Expression, purification, crystallization and preliminary X-ray crystallographic analysis of human histidine triad nucleotide-binding protein 2 (hHINT2).Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structural characterization of human histidine triad nucleotide-binding protein 2, a member of the histidine triad superfamily.The FEBS journal · 2013Article
- Kinetic mechanism of human histidine triad nucleotide binding protein 1.Biochemistry · 2013Article
- A new crystal form of human histidine triad nucleotide-binding protein 1 (hHINT1) in complex with adenosine 5'-monophosphate at 1.38 Å resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- The histidine triad nucleotide-binding protein 1 supports mu-opioid receptor-glutamate NMDA receptor cross-regulation.Cellular and molecular life sciences : CMLS · 2011Article
- NO-released zinc supports the simultaneous binding of Raf-1 and PKCγ cysteine-rich domains to HINT1 protein at the mu-opioid receptor.Antioxidants & redox signaling · 2011Article
- Hits, Fhits and Nits: beyond enzymatic function.Advances in enzyme regulation · 2011Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The three-dimensional structure of protein kinase C interacting protein 1 (PKCI-1) has been solved to high resolution by x-ray crystallography using single isomorphous replacement with anomalous scattering. The gene encoding human PKCI-1 was cloned from a cDNA library by using a partial sequence obtained from interactions identified in the yeast two-hybrid system between PKCI-1 and the regulatory domain of protein kinase C-beta. The PKCI-1 protein was expressed in Pichia pastoris as a dimer of two 13.7-kDa polypeptides. PKCI-1 is a member of the HIT family of proteins, shown by sequence identity to be conserved in a broad range of organisms including mycoplasma, plants, and humans. Despite the ubiquity of this protein sequence in nature, no distinct function has been shown for the protein product in vitro or in vivo. The PKCI-1 protomer has an alpha+beta meander fold containing a five-stranded antiparallel sheet and two helices. Two protomers come together to form a 10-stranded antiparallel sheet with extensive contacts between a helix and carboxy terminal amino acids of a protomer with the corresponding amino acids in the other protomer. PKCI-1 has been shown to interact specifically with zinc. The three-dimensional structure has been solved in the presence and absence of zinc and in two crystal forms. The structure of human PKCI-1 provides a model of this family of proteins which suggests a stable fold conserved throughout nature.
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