The new MATH: homology suggests shared binding surfaces in meprin tetramers and TRAF trimers

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, w...

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Bibliographic Details
Published in:FEBS letters 2002-10, Vol.530 (1), p.1-3
Main Authors: Sunnerhagen, Maria, Pursglove, Sharon, Fladvad, Malin
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biopolymers
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Humans
Interdomain surface
Medicin och hälsovetenskap
Membrane
Metalloendopeptidase
Models, Molecular
Molecular Sequence Data
Sequence Homology, Amino Acid
Tiopronin - chemistry
Tiopronin - metabolism
Tumor necrosis factor receptor
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)03330-6