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The new MATH: homology suggests shared binding surfaces in meprin tetramers and TRAF trimers
Author(s) -
Sunnerhagen Maria,
Pursglove Sharon,
Fladvad Malin
Publication year - 2002
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(02)03330-6
Subject(s) - homology (biology) , protein subunit , extracellular , sequence homology , homology modeling , intracellular , chemistry , biology , genetics , peptide sequence , gene , biochemistry , enzyme
Although apparently functionally unrelated, intracellular TRAFs and extracellular meprins share a region with conserved meprin and traf homology, MATH 1 . Both TRAFs and meprins require subunit assembly for function. By structural analysis of the sequences, we provide an explanation of how meprins, which form tetramers, and TRAF molecules, which form trimers, can share homology. Our analysis suggests it is highly likely that the same oligomerization surface is used. The analysis has implications for the widely distributed group of proteins containing MATH domains.