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・ Collagen, type III, alpha 1
・ Collagen, type IV, alpha 1
・ Collagen, type IX, alpha 1
・ Collagen, type V, alpha 1
・ Collagen, type VI, alpha 1
・ Collagen, type VII, alpha 1
・ Collagen, type VIII, alpha 1
・ Collagen, type X, alpha 1
・ Collagen, type XI, alpha 1
・ Collagen, type XII, alpha 1
・ Collagen, type XIII, alpha 1
・ Collagen, type XIV, alpha 1
・ Collagen, type XIX, alpha 1
・ Collagen, type XV, alpha 1
・ Collagen, type XVI, alpha 1
Collagen, type XVII, alpha 1
・ Collagen, type XVIII, alpha 1
・ Collagen, type XXIII, alpha 1
・ Collagen, type XXV, alpha 1
・ Collagen, type XXVII, alpha 1
・ Collagen-induced arthritis
・ Collagenase
・ Collagenase clostridium histolyticum
・ Collagenase IV
・ Collagenopathy, types II and XI
・ Collagenous colitis
・ Collagenous fibroma
・ Collagenous spherulosis
・ Collages (novel)
・ Collagna


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Collagen, type XVII, alpha 1 : ウィキペディア英語版
Collagen, type XVII, alpha 1

Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion.

==Structure==
Collagen XVII is a homotrimer of three alpha1(XVII)-chains and a transmembrane protein in type II orientation. Each 180 kD a-chain contains a globular intracellular domain of approximately 70 kDa, which interacts with beta4-integrin, plectin, and BP230 〔 and is necessary for the stable attachment of hemidesmosomes to keratin intermediate filaments. The large C-terminal ectodomain with a molecular mass of approximately 120 kDa consists of 15 collagenous subdomains, characterized by typical collagenous G-X-Y repeat sequences, flanked by 16 short non-collagenous stretches. The overall structure of the ectodomain is that of a flexible, rod-like triple helix with a significant thermal stability. The membrane proximal part of the ectodomain, within amino acids 506-519, is responsible for binding to alpha 6 integrin, this binding seems to be important for the collagen XVII integration into hemidesmosomes. The largest collagenous domain, Col15, which contains 232 amino acids (amino acids 567-808), contributes significantly to stability of collagen XVII homotrimer. The C-terminus of collagen XVII binds to laminin 5, and correct integration of laminin 5 into the matrix requires collagen XVII.

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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