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PDBsum entry 2epf
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Contents |
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* Residue conservation analysis
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PDB id:
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Toxin
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Title:
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Crystal structure of zinc-bound pseudecin from pseudechis porphyriacus
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Structure:
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Pseudecin. Chain: a, b, c, d. Synonym: channel blocker
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Source:
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Pseudechis porphyriacus. Red-bellied black snake. Organism_taxid: 8671. Tissue: venom
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Resolution:
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2.30Å
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R-factor:
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0.222
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R-free:
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0.277
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Authors:
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N.Suzuki,Y.Yamazaki,Z.Fujimoto,T.Morita,H.Mizuno
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Key ref:
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N.Suzuki
et al.
(2008).
Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain.
Acta Crystallogr D Biol Crystallogr,
64,
1034-1042.
PubMed id:
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Date:
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29-Mar-07
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Release date:
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11-Mar-08
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PROCHECK
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Headers
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References
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Q8AVA3
(CRVP_PSEPO) -
Cysteine-rich venom protein pseudecin from Pseudechis porphyriacus
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Seq:
Struc:
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238 a.a.
207 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Acta Crystallogr D Biol Crystallogr
64:1034-1042
(2008)
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PubMed id:
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Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain.
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N.Suzuki,
Y.Yamazaki,
R.L.Brown,
Z.Fujimoto,
T.Morita,
H.Mizuno.
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ABSTRACT
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Cyclic nucleotide-gated (CNG) ion channels play pivotal roles in sensory
transduction by retinal photoreceptors and olfactory neurons. The elapid snake
toxins pseudechetoxin (PsTx) and pseudecin (Pdc) are the only known protein
blockers of CNG channels. These toxins belong to a cysteine-rich secretory
protein (CRISP) family containing an N-terminal pathogenesis-related proteins of
group 1 (PR-1) domain and a C-terminal cysteine-rich domain (CRD). PsTx and Pdc
are highly homologous proteins, but their blocking affinities on CNG channels
are different: PsTx blocks both the olfactory and retinal channels with
approximately 15-30-fold higher affinity than Pdc. To gain further insights into
their structure and function, the crystal structures of PsTx, Pdc and Zn2+-bound
Pdc were determined. The structures revealed that most of the amino-acid-residue
differences between PsTx and Pdc are located around the concave surface formed
between the PR-1 domain and the CRD, suggesting that the concave surface is
functionally important for CNG-channel binding and inhibition. A structural
comparison in the presence and absence of Zn2+ ion demonstrated that the concave
surface can open and close owing to movement of the CRD upon Zn2+ binding. The
data suggest that PsTx and Pdc occlude the pore entrance and that the dynamic
motion of the concave surface facilitates interaction with the CNG channels.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.J.Koppers,
T.Reddy,
and
M.K.O'Bryan
(2011).
The role of cysteine-rich secretory proteins in male fertility.
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Asian J Androl,
13,
111-117.
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O.A.Asojo
(2011).
Structure of a two-CAP-domain protein from the human hookworm parasite Necator americanus.
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Acta Crystallogr D Biol Crystallogr,
67,
455-462.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
