4cml: Difference between revisions

Revision as of 07:03, 21 May 2014

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

Structural highlights

4cml is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	52N, CL, GOL, MG, SO4
Related:	4cmn
Activity:	Phosphoinositide 5-phosphatase, with EC number 3.1.3.36
Resources:	FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

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.

Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases.,Tresaugues L, Silvander C, Flodin S, Welin M, Nyman T, Graslund S, Hammarstrom M, Berglund H, Nordlund P Structure. 2014 Apr 2. pii: S0969-2126(14)00073-2. doi:, 10.1016/j.str.2014.01.013. PMID:24704254^[1]

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.

References

↑ Tresaugues L, Silvander C, Flodin S, Welin M, Nyman T, Graslund S, Hammarstrom M, Berglund H, Nordlund P. Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases. Structure. 2014 Apr 2. pii: S0969-2126(14)00073-2. doi:, 10.1016/j.str.2014.01.013. PMID:24704254 doi:https://dx.doi.org/10.1016/j.str.2014.01.013

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OCA

[1] Tresaugues L, Silvander C, Flodin S, Welin M, Nyman T, Graslund S, Hammarstrom M, Berglund H, Nordlund P. Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases. Structure. 2014 Apr 2. pii: S0969-2126(14)00073-2. doi:, 10.1016/j.str.2014.01.013. PMID:24704254 doi:https://dx.doi.org/10.1016/j.str.2014.01.013

[1]

@@ Line 1: / Line 1: @@
-{{STRUCTURE_4cml|  PDB=4cml  |  SCENE=  }}
+==Crystal Structure of INPP5B in complex with Phosphatidylinositol 3,4- bisphosphate==
-===Crystal Structure of INPP5B in complex with Phosphatidylinositol 3,4- bisphosphate===
+<StructureSection load='4cml' size='340' side='right' caption='[[4cml]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-{{ABSTRACT_PUBMED_24704254}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4cml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CML FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=52N:1,2-DIOCTANOYL+PHOSPHATIDYL+EPI-INOSITOL+(3,4)-BISPHOSPHATE'>52N</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cmn|4cmn]]</td></tr>
+<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoinositide_5-phosphatase Phosphoinositide 5-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.36 3.1.3.36] </span></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cml RCSB], [http://www.ebi.ac.uk/pdbsum/4cml PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Function==
+Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases.,Tresaugues L, Silvander C, Flodin S, Welin M, Nyman T, Graslund S, Hammarstrom M, Berglund H, Nordlund P Structure. 2014 Apr 2. pii: S0969-2126(14)00073-2. doi:, 10.1016/j.str.2014.01.013. PMID:24704254<ref>PMID:24704254</ref>
-[[http://www.uniprot.org/uniprot/I5P2_HUMAN I5P2_HUMAN]] Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.<ref>PMID:7721860</ref>
-==About this Structure==
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-[[4cml]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CML OCA].
+</div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:024704254</ref><references group="xtra"/><references/>
+__TOC__
+</StructureSection>
+[[Category: Human]]
 [[Category: Phosphoinositide 5-phosphatase]]
 [[Category: Arrowsmith, C H.]]

4cml: Difference between revisions

Revision as of 07:03, 21 May 2014

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

Structural highlights

Publication Abstract from PubMed

References

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