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UCP2 is 309 amino acids long with domains located in the mitochondrial matrix, in the inner mitochondrial membrane and in the intermembrane mitochondrial space. | UCP2 is 309 amino acids long with domains located in the mitochondrial matrix, in the inner mitochondrial membrane and in the intermembrane mitochondrial space. | ||
More precisely it can be described as a chain of six transmembrane helices and three amphipathic helices. The structure consists of three pseudo-repeats in which a transmembrane helix is linked by a loop to an amphipathic helix, followed by another transmembrane alpha helix. <ref>Kream, E., Mitochondrial uncoupling protein 2 [https://collab.its.virginia.edu/access/content/group/f85bed6c-45d2-4b18-b868-6a2353586804/2/Ch20_Kream_E_Uncoupling_Protein_2_(Mitochondrial)-_-/Ch20_Kream_E_Uncoupling_Protein_2_(Mitochondrial)_MitochondrialUncouplingProtein2.html]<ref/> | More precisely it can be described as a chain of six transmembrane helices and three amphipathic helices. The structure consists of three pseudo-repeats in which a transmembrane helix is linked by a loop to an amphipathic helix, followed by another transmembrane alpha helix. <ref>Kream, E., Mitochondrial uncoupling protein 2 [https://collab.its.virginia.edu/access/content/group/f85bed6c-45d2-4b18-b868-6a2353586804/2/Ch20_Kream_E_Uncoupling_Protein_2_(Mitochondrial)-_-/Ch20_Kream_E_Uncoupling_Protein_2_(Mitochondrial)_MitochondrialUncouplingProtein2.html]<ref/> | ||
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In addition, transmembrane helices are mainly composed of Hydrophobic amino acids with a lot of alanine, valine and leucine. <ref>[https://www.uniprot.org/uniprot/P70406] UniProtKB - P70406 UCP2_MOUSE <ref/> | In addition, transmembrane helices are mainly composed of Hydrophobic amino acids with a lot of alanine, valine and leucine. <ref>[https://www.uniprot.org/uniprot/P70406] UniProtKB - P70406 UCP2_MOUSE <ref/> | ||
Membrane-protein structure determination and characterisation of UCP2 is a difficulty which is overcomed thanks to a specific NMR method. This method combines two technics : first, the use of NMR residual dipolar couplings (RDCs) which give orientation restraints and Paramagnetic Relaxation Enhancement (PRE) which determines distance restraints. Experimental RDCs of UCP2 were compared to assemblies of known molecular fragments (from the Protein Data Bank) aiming the determination of the local and secondary structures. Moreover, PRE restraints provide their spatial arrangement in the tertiary fold. <ref>Ricquier, D., Bouillaud, F., (2000) The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220743/pdf/10620491.pdf]<ref/> | Membrane-protein structure determination and characterisation of UCP2 is a difficulty which is overcomed thanks to a specific NMR method. This method combines two technics : first, the use of NMR residual dipolar couplings (RDCs) which give orientation restraints and Paramagnetic Relaxation Enhancement (PRE) which determines distance restraints. Experimental RDCs of UCP2 were compared to assemblies of known molecular fragments (from the Protein Data Bank) aiming the determination of the local and secondary structures. Moreover, PRE restraints provide their spatial arrangement in the tertiary fold. <ref>Ricquier, D., Bouillaud, F., (2000) The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220743/pdf/10620491.pdf]<ref/> | ||
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UCP2
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The UCP2 protein is a transmembrane protein found in mitochondrias in different tissues such as white adipose and muscular tissues. This protein allows an uncoupling of the electrochemical potential of membrane in the respiratory chain of mitochondria resulting in a heat creation. This protein is a carrier of protons and chlorides.
A transmembrane protein
UCP2 is 309 amino acids long with domains located in the mitochondrial matrix, in the inner mitochondrial membrane and in the intermembrane mitochondrial space. More precisely it can be described as a chain of six transmembrane helices and three amphipathic helices. The structure consists of three pseudo-repeats in which a transmembrane helix is linked by a loop to an amphipathic helix, followed by another transmembrane alpha helix. [1]
