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PDBsum entry 3wxa
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Apoptosis/transport protein
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PDB id
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3wxa
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References listed in PDB file
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Key reference
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Title
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Structural analysis of the complex between penta-Ef-Hand alg-2 protein and sec31a peptide reveals a novel target recognition mechanism of alg-2.
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Authors
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T.Takahashi,
K.Kojima,
W.Zhang,
K.Sasaki,
M.Ito,
H.Suzuki,
M.Kawasaki,
S.Wakatsuki,
T.Takahara,
H.Shibata,
M.Maki.
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Ref.
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Int J Mol Sci, 2015,
16,
3677-3699.
[DOI no: ]
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PubMed id
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Abstract
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ALG-2, a 22-kDa penta-EF-hand protein, is involved in cell death, signal
transduction, membrane trafficking, etc., by interacting with various proteins
in mammalian cells in a Ca2+-dependent manner. Most known ALG-2-interacting
proteins contain proline-rich regions in which either PPYPXnYP (type 1 motif) or
PXPGF (type 2 motif) is commonly found. Previous X-ray crystal structural
analysis of the complex between ALG-2 and an ALIX peptide revealed that the
peptide binds to the two hydrophobic pockets. In the present study, we resolved
the crystal structure of the complex between ALG-2 and a peptide of Sec31A
(outer shell component of coat complex II, COPII; containing the type 2 motif)
and found that the peptide binds to the third hydrophobic pocket (Pocket 3).
While amino acid substitution of Phe85, a Pocket 3 residue, with Ala abrogated
the interaction with Sec31A, it did not affect the interaction with ALIX. On the
other hand, amino acid substitution of Tyr180, a Pocket 1 residue, with Ala
caused loss of binding to ALIX, but maintained binding to Sec31A. We conclude
that ALG-2 recognizes two types of motifs at different hydrophobic surfaces.
Furthermore, based on the results of serial mutational analysis of the
ALG-2-binding sites in Sec31A, the type 2 motif was newly defined.
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