Claim · model-written summary
The mature MsPR-1b has a pI of 9.4.
- Taxon
- Mucuna sempervirens
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Mucuna sempervirenst0 - Gene
- MsPR-1be1
- Outcome
- pIe1
- Value
- 9.4e1
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
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Verbatim
t0“Mucuna sempervirens”
e1“The mature MsPR-1b is a small basic secreted protein (15 134 Da, pI 9.4) that lacks glycosylation”
Title
Hong-Guang Zha; Peng Cui; Ying Yu; et al. Annals of Botany 2026. doi:10.1093/aob/mcag015
Other claims from this paper (9)
- Observation The MsPR-1b gene of Mucuna sempervirens encodes a 164-amino-acid precursor with an N-terminal signal peptide.
- Observation MsPR-1b expression in Mucuna sempervirens was detected predominantly in the nectary.
- Observation The mature MsPR-1b is a small basic secreted protein of 15 134 Da.
- Observation The mature MsPR-1b lacks glycosylation.
- Observation The crystal structure of native MsPR-1b, the first native PR-1 protein purified from its natural source, revealed a homodimer.
- Observation Each MsPR-1b monomer adopts the conserved α-β-α sandwich fold characteristic of the CAP superfamily.
- Observation Each MsPR-1b monomer contains two intrachain disulphide bonds.
- Observation MsPR-1b displayed no detectable lipid-binding capacity or direct antimicrobial activity.
- Mechanism The authors suggest that nectar-secreted PR-1s might perform specialized, non-defensive functions distinct from canonical pathogen-related roles.