Words similar to carboxyl-terminal
- carbon-dating
- carbondale
- carbonizzato
- carboxy-tetramethyl-rhodamine
- carboxyethyl
- carboxyfluorescein
- carboxykinase
- carboxyl
- carboxyl-activated
- carboxyl-terminal
- carboxyl-termini
- carboxyl-terminus
- carboxylase
- carboxylases
- carboxylate
- carboxylesterase
- carboxymethyl-
- carboxymethyl-lysine
- carbón
- carcaterra
Example sentences for: carboxyl-terminal
How can you use “carboxyl-terminal” in a sentence? Here are some example sentences to help you improve your vocabulary:
3), containing half of the anaphylatoxin type I repeats, an EGF-adjoining sequence, calcium-binding EGF-like modules and a carboxyl-terminal fibulin-type module, demonstrated interaction with the extracellular domain of proHB-EGF (Additional file 1).
The site of fibulin-1 binding to laminin maps to the carboxyl-terminal segment of the laminin A chain which consists of five basic tandem repeats containing conserved glycine and cysteine residues [ 39 46 ] . The binding site of laminin to fibulin-1 maps to the calcium-binding type II EGF-like modules of fibulin-1 [ 39 ] .
There are two homologous type IA topoisomerases present in E. coli . Topoisomerase III has potent DNA decatenating activity for resolution of plasmid DNA replication intermediates, but much weaker relaxation activity than topoisomerase I [ 17 ] . To exhibit maximal relaxation activity, topoisomerase III requires high temperature (52°C) along with low magnesium and monovalent ion [ 17 18 ] . In contrast, E. coli topoisomerase I was not active in the in vitro assay for resolution of plasmid DNA replication intermediates [ 19 ] . Removal of the C-terminal 49 amino acids from the 653 amino acid topoisomerase III protein resulted in drastic reduction of catalytic activity [ 20 ] . Fusion of the carboxyl-terminal 312 amino acid residues of E. coli topoisomerase I, which includes the entire ZD domain, onto the 605 N-terminal amino acids of topoisomerase III generated a hybrid topoisomerase that has relaxation activity resembling topoisomerase III along with weak decatenating activity [ 21 ] . Although preferring single-stranded DNA as binding substrate, topoisomerase I had been shown to also bind double-stranded DNA [ 22 ] , but there is no data available to indicate which domain in the enzyme is responsible for this interaction.
AtCOP1 contains three conserved structural domains: a RING finger at the amino terminus, a coiled-coil domain in the middle, and a carboxyl-terminal WD40 repeat domain [ 9 10 ] . Each of the three conserved domains has been shown to mediate protein-protein interactions [ 11 12 13 ] . The subcellular localization of AtCOP1 is regulated by light in a tissue specific manner [ 14 15 ] . The hypocotyl cell nuclei contain high levels of COP1 in the dark and reduced levels in the light, suggesting that the nucleocytoplasmic partitioning of AtCOP1 is adjusted by a light-responsive mechanism [ 14 16 ] . The activity of AtCOP1 is at least in part regulated by its subcellular localization, as the degradation of HY5 is dependent upon the nuclear accumulation of AtCOP1 in the dark [ 4 ] . AtCOP1 was demonstrated to carry a single, bipartite nuclear localization signal located between the coiled-coil domain and the WD-40 domain (amino acid 294-314) and a cytoplasmic localization signal, which was mapped to a region partially overlapping with the RING finger and the coiled-coil domain (amino acid 67-117) [ 17 ] . Strikingly, AtCOP1 protein forms characteristic nuclear speckles when transiently expressed in onion epidermal cells or stably expressed in transgenic Arabidopsis [ 6 18 ] . The functional role of these speckles is currently unknown; however, a subnuclear localization signal consisting of 58 residues (amino acid 120-177) is required for their formation [ 19 ] .
Nidogen is a basement membrane protein composed of three globular domains G1-G3 and two linking sequences; domain G1 is joined to domain G2 through a flexible link and domain G2 is connected to domain G3 by a rod-like element consisting of EGF-like modules [ 47 ] . Nidogen1 is an important structural component of tertiary complexes with other such extracellular components as laminins, collagen IV, perlecan, and fibulins [ 48 ] . Fibulin-1C binds to nidogen1 through domain G2 of nidogen [ 48 ] . The nidogen binding site of fibulin-1C includes the type II EGF-like modules 6-9 and the carboxyl-terminal domain [ 42 ] .
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