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A model for Batten disease protein CLN3: Functional implications from homology and mutations
Author(s) -
Janes Robert W.,
Munroe Patricia B.,
Mitchison Hannah M.,
Mark Gardiner R.,
Mole Sara E.,
Wallace B.A.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01290-2
Subject(s) - batten disease , biology , homology modeling , yarrowia , protein subunit , protein folding , homology (biology) , peptide sequence , atp synthase , biochemistry , genetics , gene , microbiology and biotechnology , enzyme
In an attempt to understand the molecular nature of Batten disease, we have examined the amino acid sequence of the affected CLN3 gene product (The International Batten Disease Consortium (1995) Cell 82, 949–957) and the site‐specific mutations which give rise to the biological defect. Homology searches and molecular modeling have led to the development of a model for the folding and disposition of the protein, possibly within a mitochondrial membrane. High homology with a yeast protein of unknown function suggests a strong evolutionary conservation of function. We speculate that a possible role for the protein may be in chaperoning the folding/unfolding or assembly/disassembly of other proteins, specifically subunit c of the mitochondrial ATP synthase complex.