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Crystal stuctures of MglB‐2 (TP0684), a topologically variant d‐glucose‐binding protein from Treponema pallidum, reveal a ligand‐induced conformational change
Previously, we determined the crystal structure of apo‐TpMglB‐2, a d‐glucose‐binding component of a putative ABC transporter from the syphilis spirochete Treponema pallidum. The protein had an unusual topology for this class of proteins, raising the question of whether the d‐glucose‐binding mode wou...
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| Vydáno v: | Protein Sci |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
John Wiley and Sons Inc.
2018
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5866939/ https://ncbi.nlm.nih.gov/pubmed/29318719 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.3373 |
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