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The thrombospondin‐like chains of cartilage oligomeric matrix protein are assembled by a five‐stranded α‐helical bundle between residues 20 and 83
Author(s) -
Efimov Vladimir P.,
Lustig Ariel,
Engel Jürgen
Publication year - 1994
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 - 10.1016/0014-5793(94)80239-4
Subject(s) - thrombospondin , cartilage oligomeric matrix protein , chemistry , cartilage , viral matrix protein , bundle , matrix (chemical analysis) , biophysics , crystallography , materials science , biochemistry , anatomy , biology , medicine , matrix metalloproteinase , composite material , pathology , chromatography , alternative medicine , metalloproteinase , gene , osteoarthritis
The N‐terminal fragment of rat cartilage oligomeric matrix protein (COMP), comprising residues 20–83, was over‐expressed in E. coli and purified under non‐denaturing conditions. The fragment forms pentamers similar to the assembly domain of the native protein. Its five chains can be covalently linked in vitro by oxidation of cysteines 68 and 71. The fragment adopts a predominantly α‐helical structure as judged by circular dichroism spectroscopy. On the basis of these findings we propose the model of a five‐stranded α‐helical bundle for the assembly domain of COMP. The studied sequence is conserved in thrombospondins 3 and 4 thus raising the possibility that these proteins are also pentamers.