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| {{STRUCTURE_1w2d| PDB=1w2d | SCENE= }} | | {{STRUCTURE_1w2d| PDB=1w2d | SCENE= }} |
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| '''HUMAN INOSITOL (1,4,5)-TRISPHOSPHATE 3-KINASE COMPLEXED WITH MN2+/ADP/INS(1,3,4,5)P4'''
| | ===HUMAN INOSITOL (1,4,5)-TRISPHOSPHATE 3-KINASE COMPLEXED WITH MN2+/ADP/INS(1,3,4,5)P4=== |
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| ==Overview==
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| Mammalian cells produce a variety of inositol phosphates (InsPs), including Ins(1,4,5)P3 that serves both as a second messenger and as a substrate for inositol polyphosphate kinases (IPKs), which further phosphorylate it. We report the structure of an IPK, the human Ins(1,4,5)P3 3-kinase-A, both free and in complexes with substrates and products. This enzyme catalyzes transfer of a phosphate from ATP to the 3-OH of Ins(1,4,5)P3, and its X-ray crystal structure provides a template for understanding a broad family of InsP kinases. The catalytic domain consists of three lobes. The N and C lobes bind ATP and resemble protein and lipid kinases, despite insignificant sequence similarity. The third lobe binds inositol phosphate and is a unique four-helix insertion in the C lobe. This lobe embraces all of the phosphates of Ins(1,4,5)P3 in a positively charged pocket, explaining the enzyme's substrate specificity and its inability to phosphorylate PtdIns(4,5)P2, the membrane-resident analog of Ins(1,4,5)P3.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15350214}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15350214 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15350214}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ip4]] | | [[Category: Ip4]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:03:24 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:47:31 2008'' |
