FEBS Letters · 2000 · 129 citations · 19 references
Life SciencesBiochemistryMolecular BiologyGene ExpressionProtein-protein InteractionsStructural BiologyProtein DimerizationProtein Interaction DomainsProtein OligomerizationProtein StructureMulti-domain ProteinsMultimeric Protein AssemblyOligomerization MechanismsProtein Domain ClassificationProtein Domain OrganizationReporter Gene AssaysReporter Gene Construction
The N-terminal cysteine-rich domain (EMI domain) of EMILIN-1 is a new protein domain that is shared with two proteins (multimerin and EMILIN-2) and with four additional database entries. The EMI domains are always located at the N-terminus, have a common gene organization, and belong to proteins that are forming or are compatible with multimer formation. The potential role of the EMI domain in the assembly of EMILIN-1 was investigated by the two-hybrid system. No reporter gene activity was detected when EMI-1 was co-transformed with the C-terminal gC1q-1 domain excluding a head-to-tail multimerization; conversely, a strong interaction was detected when the EMI-1 domain was co-transformed with the gC1q-2 domain of EMILIN-2.
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Prediction of complete gene structures in human genomic DNA
Chris Burge, Samuel Karlin · Journal of Molecular Biology · 1997 · 4.3K citations