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Structure of the aquaporin‐0 mediated membrane junction
Author(s) -
Gonen Tamir
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a208-d
Subject(s) - aquaporin , membrane , electron crystallography , biophysics , water channel , membrane protein , chemistry , membrane structure , cell membrane , resolution (logic) , microbiology and biotechnology , crystallography , biochemistry , biology , optics , physics , computer science , electron diffraction , inlet , mechanical engineering , engineering , artificial intelligence , diffraction
We present the structure of aquaporin‐0, a water channel that is only found in the eye lens, and has two unique functions: it forms a water selective pore in membranes, and acts as an adhesive protein, forming cell‐to‐cell membrane junctions. We determined the structure of the AQP0 mediated membrane junction to 1.9Å resolution by electron crystallography, and present the structure of a shell of annular lipids surrounding the protein.