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.
Read more about this topic: Collagen, Type XVII, Alpha 1
Famous quotes containing the word structure:
“... the structure of our public morality crashed to earth. Above its grave a tombstone read, “Be tolerant—even of evil.” Logically the next step would be to say to our commonwealth’s criminals, “I disagree that it’s all right to rob and murder, but naturally I respect your opinion.” Tolerance is only complacence when it makes no distinction between right and wrong.”
—Sarah Patton Boyle, U.S. civil rights activist and author. The Desegregated Heart, part 2, ch. 2 (1962)
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—Donald Davidson (b. 1917)