4CML: Crystal Structure of INPP5B in complex with Phosphatidylinositol 3,4- bisphosphate

Citation:
Abstract
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.
PDB ID: 4CMLDownload
MMDB ID: 119162
PDB Deposition Date: 2014/1/16
Updated in MMDB: 2014/05
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 4CML: trimeric; determined by author and by software (PISA)
Molecular Components in 4CML
Label Count Molecule
Proteins (3 molecules)
3
Type II Inositol 1,4,5-trisphosphate 5- Phosphatase, Isoform 2(Gene symbol: INPP5B)
Molecule annotation
Chemicals (15 molecules)
1
3
2
3
3
3
4
3
5
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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