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PDBsum entry 1aii
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Calcium/phospholipid binding protein
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PDB id
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1aii
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References listed in PDB file
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Key reference
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Title
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Can enzymatic activity, Or otherwise, Be inferred from structural studies of annexin III?
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Authors
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B.Perron,
A.Lewit-Bentley,
B.Geny,
F.Russo-Marie.
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Ref.
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J Biol Chem, 1997,
272,
11321-11326.
[DOI no: ]
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PubMed id
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Abstract
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Annexin III, a putative inositol (1,2)-phosphohydrolase, was co-crystallized
with inositol 2-phosphate, the inhibitor of the reaction, and its structure was
solved to 1.95 A resolution. No enzyme active site was observed in the
structure. Assays for enzymatic activity were also negative. Search for annexin
III-inositol phosphate interactions using the BIAcoreTM system revealed an
affinity for inositol cyclic (1,2)-phosphate, suggesting annexin III may
sequester the molecule in the cell. The BIAcoreTM system used with different
phospholipids showed that annexin III displays specificity for
phosphatidylethanolamine, but not for phosphatidylinositols. Interestingly, a
molecule of ethanolamine was found bound to the protein in the crystal
structure. Coupled with the fact that this is a particularly abundant
phospholipid in granules specific to neutrophils, cells where annexin III is
highly expressed, our finding could be pointing to a physiological role of
annexin III.
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Figure 4.
Fig. 4. Superposition of the C  backbone of
native annexin III (black) on annexin III with inositol
2-phosphate in the crystallization medium (gray), viewed down
the local 2-fold axis (figure prepared^ using the MOLSCRIPT
program (33)).
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Figure 5.
Fig. 5. A model of the interaction of the third domain in
annexin III with phospholipids. The position of the
ethanolamine^ group is given by our results, that of the
phosphate of the phosphatidyl^ serine from analogy with the
sulfate ion interacting with the^ principal calcium site in
annexin V (26). The phosphatidylserine^ coordinates were kindly
supplied by A. Sanson (34). Calcium^ ions are red,
phosphatidylserine is dark blue, phosphatidylethanolamine^ is
green, and the Trp-191 side chain is cyan.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(1997,
272,
11321-11326)
copyright 1997.
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