2ki3
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Structural and biochemical characterization of FK506 binding domain from Plasmodium vivax
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Structural highlights
FunctionEvolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPvFKBP35 is a member of the FK506 binding protein family (FKBP) from Plasmodium vivax. The FK506-binding domain of PvFKBP35 shows a canonical peptidylprolyl cis-trans isomerase (PPIase) activity. To understand the role of PvFKBP35 in the parasite, we have performed NMR studies. Here, we report the assignment of the FK506-binding domain of PvFKBP35. NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax.,Alag R, Shin J, Yoon HS Biomol NMR Assign. 2009 Dec;3(2):243-5. PMID:19774494[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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