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Crystal Structure of Arabidopsis Cyclophilin38 Reveals a Previously Uncharacterized Immunophilin Fold and a Possible Autoinhibitory Mechanism([W])
Cyclophilin38 (CYP38) is one of the highly divergent cyclophilins from Arabidopsis thaliana. Here, we report the crystal structure of the At-CYP38 protein (residues 83 to 437 of 437 amino acids) at 2.39-Å resolution. The structure reveals two distinct domains: an N-terminal helical bundle and a C-te...
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| Autori principali: | , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society of Plant Biologists
2012
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3406915/ https://ncbi.nlm.nih.gov/pubmed/22706283 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1105/tpc.111.093781 |
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