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・ Peptidoglycan-N-acetylglucosamine deacetylase
・ Peptidomimetic
・ Peptidyl transferase
・ Peptidyl-Asp metalloendopeptidase
・ Peptidyl-dipeptidase B
・ Peptidyl-dipeptidase Dcp
・ Peptidyl-glutamate 4-carboxylase
・ Peptidyl-glutaminase
・ Peptidyl-glycinamidase
・ Peptidyl-L-lysine(-L-arginine) hydrolase
・ Peptidyl-Lys metalloendopeptidase
・ Peptidylamidoglycolate lyase
・ Peptidylglycine alpha-amidating monooxygenase
・ Peptidylglycine monooxygenase
・ Peptidylprolyl isomerase A
Peptidylprolyl isomerase D
・ Peptitergents
・ Peptization
・ Peptococcaceae
・ Peptococcus
・ Peptoid
・ Peptoid nanosheet
・ Peptoniphilus
・ Peptostreptococcaceae
・ Peptostreptococcus
・ Peptostreptococcus anaerobius
・ Peptostreptococcus asaccharolyticus
・ Pepu Hernández
・ Pepusch
・ Pepuza


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Peptidylprolyl isomerase D : ウィキペディア英語版
Peptidylprolyl isomerase D

Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the ''PPID'' gene on chromosome 4. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPID participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer.
==Structure==
Like other cyclophilins, PPID forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti-parallel β-strands and capped by two α-helices at the top and bottom. In addition, the β-turns and loops in the strands contribute to the flexibility of the barrel.〔 PPID in particular is composed of 370 residues and shares structural homology with PPIF, FKBP51, and FKBP52, including an N-terminal immunophilin-like domain and a C-terminal tetratricopeptide repeat (TPR) domain.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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