Target type: molecularfunction
Binding to a protein or protein complex, in the presence of copper. [GOC:ecd, PMID:16884690]
Copper-dependent protein binding is a molecular function that involves the interaction of a protein with copper ions. Copper is an essential trace metal that plays a critical role in a variety of biological processes, including cellular respiration, antioxidant defense, and neurotransmission. Copper-dependent proteins typically contain one or more copper binding sites, which are often located in specific structural domains. These binding sites can vary in their coordination chemistry and can be composed of amino acid residues such as histidine, cysteine, and methionine. The binding of copper to these sites can induce conformational changes in the protein, which can alter its activity or stability. In some cases, copper binding can also facilitate the formation of protein complexes. The precise molecular function of copper-dependent protein binding depends on the specific protein and its role in the cell. For example, some copper-dependent proteins function as enzymes, while others act as structural components or signaling molecules. Understanding the molecular function of copper-dependent protein binding is crucial for understanding the role of copper in human health and disease. Copper deficiency or overload can lead to various pathological conditions, such as anemia, neurodegeneration, and cardiovascular disease. Studying the interaction of copper with proteins can provide insights into the mechanisms underlying these diseases and may facilitate the development of novel therapeutic strategies.'
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Protein | Definition | Taxonomy |
---|---|---|
Peptidyl-prolyl cis-trans isomerase FKBP4 | A peptidyl-prolyl cis-trans isomerase FKBP4 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q02790] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
cycloheximide | cycloheximide : A dicarboximide that is 4-(2-hydroxyethyl)piperidine-2,6-dione in which one of the hydrogens attached to the carbon bearing the hydroxy group is replaced by a 3,5-dimethyl-2-oxocyclohexyl group. It is an antibiotic produced by the bacterium Streptomyces griseus. Cycloheximide: Antibiotic substance isolated from streptomycin-producing strains of Streptomyces griseus. It acts by inhibiting elongation during protein synthesis. | antibiotic fungicide; cyclic ketone; dicarboximide; piperidine antibiotic; piperidones; secondary alcohol | anticoronaviral agent; bacterial metabolite; ferroptosis inhibitor; neuroprotective agent; protein synthesis inhibitor |
3-(3-pyridyl)-1-propyl-(2s)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-pyrrolidinecarboxylate | |||
biricodar | biricodar: a non-macrocyclic ligand for FKBP12; structure in first source | alpha-amino acid ester | |
pd 407824 | |||
l 683590 | immunomycin: from Streptomyces hygroscopicus; structure given in first source | ether; lactol; macrolide; secondary alcohol | antifungal agent; bacterial metabolite; immunosuppressive agent |
cyclosporine | ramihyphin A: one of the metabolites produced by Fusarium sp. S-435; RN given refers to cpd with unknown MF | homodetic cyclic peptide | anti-asthmatic drug; anticoronaviral agent; antifungal agent; antirheumatic drug; carcinogenic agent; dermatologic drug; EC 3.1.3.16 (phosphoprotein phosphatase) inhibitor; geroprotector; immunosuppressive agent; metabolite |
timcodar | timcodar: a mutlidrug resistance inhibitor; structure in first source |