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PDBsum entry 3mtc
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Hydrolase/hydrolase inhibitor
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PDB id
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3mtc
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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 basis for phosphoinositide substrate recognition, Catalysis, And membrane interactions in human inositol polyphosphate 5-Phosphatases.
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Authors
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L.Trésaugues,
C.Silvander,
S.Flodin,
M.Welin,
T.Nyman,
S.Gräslund,
M.Hammarström,
H.Berglund,
P.Nordlund.
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Ref.
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Structure, 2014,
22,
744-755.
[DOI no: ]
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PubMed id
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Abstract
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SHIP2, OCRL, and INPP5B belong to inositol polyphosphate 5-phophatase
subfamilies involved in insulin regulation and Lowes syndrome. The structural
basis for membrane recognition, substrate specificity, and regulation of
inositol polyphosphate 5-phophatases is still poorly understood. We determined
the crystal structures of human SHIP2, OCRL, and INPP5B, the latter in complex
with phosphoinositide substrate analogs, which revealed a membrane interaction
patch likely to assist in sequestering substrates from the lipid bilayer.
Residues recognizing the 1-phosphate of the substrates are highly conserved
among human family members, suggesting similar substrate binding modes. However,
3- and 4-phosphate recognition varies and determines individual substrate
specificity profiles. The high conservation of the environment of the scissile
5-phosphate suggests a common reaction geometry for all members of the human
5-phosphatase family.
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