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The new MATH: homology suggests shared binding surfaces in meprin tetramers and TRAF trimers
- Source :
- FEBS Letters. (1-3):1-3
- Publisher :
- Published by Elsevier B.V.
-
Abstract
- Although apparently functionally unrelated, intracellular TRAFs and extracellular meprins share a region with conserved meprin and traf homology, MATH1. 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.
- Subjects :
- Models, Molecular
Protein subunit
Molecular Sequence Data
Biophysics
Computational biology
Biology
Biochemistry
Homology (biology)
Biopolymers
Structural Biology
Metalloendopeptidase
Genetics
Humans
Amino Acid Sequence
Molecular Biology
Sequence Homology, Amino Acid
Tiopronin
Membrane
Cell Biology
Interdomain surface
MATH domain
Carrier Proteins
Tumor necrosis factor receptor
Function (biology)
Intracellular
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 1-3
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....823a6aaf34aee686fb3c240bf5b5b296
- Full Text :
- https://doi.org/10.1016/S0014-5793(02)03330-6