翻訳と辞書 ・ 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.
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