Folding and stability of the aquaglyceroporin GlpF: Implications for human aqua(glycero)porin diseases
作者： Noreen Klein , Jennifer Neumann , Joe D. O'Neil , Dirk Schneider
DOI: 10.1016/J.BBAMEM.2014.11.015
关键词: Endoplasmic-reticulum-associated protein degradation 、 Transmembrane protein 、 Cell biology 、 Chemistry 、 Membrane protein 、 Folding (chemistry) 、 Protein structure 、 Biochemistry 、 Aquaporin 、 Protein folding 、 Porin
摘要: Aquaporins are highly selective polytopic transmembrane channel proteins that facilitate the permeation of water across cellular membranes in a large diversity organisms. Defects aquaporin function associated with common diseases, such as nephrogenic diabetes insipidus, congenital cataract and certain types cancer. In general, aquaporins have conserved structure; from prokaryotes to humans. The structure, together structural dynamics framework for substrate selectivity is discussed. folding pathway has been topic several studies recent years. These revealed protein structure can be reached by following different pathways. Based on available data, we suggest complex aquaporins, starting insertion individual helices up formation tetrameric structure. consequences some known mutations human aquaporin-encoding genes, which most likely affect stability
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