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Differential substrate recognition by maltose binding proteins influenced by structure and dynamics
The genome of the hyperthermophile Thermotoga maritima contains three isoforms of maltose binding protein (MBP) that are high affinity receptors for di-, tri- and tetra-saccharides. Two of these proteins (tmMBP1 and tmMBP2) share significant sequence identity, approximately 90%, while the third (tmM...
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| Published in: | Biochemistry |
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| Main Authors: | , , , , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
2018
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6189639/ https://ncbi.nlm.nih.gov/pubmed/30204415 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.8b00783 |
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