1jk7
From Proteopedia
(New page: 200px<br /> <applet load="1jk7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jk7, resolution 1.90Å" /> '''CRYSTAL STRUCTURE O...) |
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caption="1jk7, resolution 1.90Å" /> | caption="1jk7, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF THE TUMOR-PROMOTER OKADAIC ACID BOUND TO PROTEIN PHOSPHATASE-1'''<br /> | '''CRYSTAL STRUCTURE OF THE TUMOR-PROMOTER OKADAIC ACID BOUND TO PROTEIN PHOSPHATASE-1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MN, SO4, OKA and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http:// | + | 1JK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=OKA:'>OKA</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JK7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase-inhibitor complex]] | [[Category: hydrolase-inhibitor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:07:46 2008'' |
Revision as of 14:07, 15 February 2008
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CRYSTAL STRUCTURE OF THE TUMOR-PROMOTER OKADAIC ACID BOUND TO PROTEIN PHOSPHATASE-1
Overview
Protein phosphatase-1 (PP1) plays a key role in dephosphorylation in, numerous biological processes such as glycogen metabolism, cell cycle, regulation, smooth muscle contraction, and protein synthesis., Microorganisms produce a variety of inhibitors of PP1, which include the, microcystin class of inhibitors and okadaic acid, the latter being the, major cause of diarrhetic shellfish poisoning and a powerful tumor, promoter. We have determined the crystal structure of the molecular, complex of okadaic acid bound to PP1 to a resolution of 1.9 A. This, structure reveals that the acid binds in a hydrophobic groove adjacent to, the active site of the protein and interacts with basic residues within, the active site. Okadaic acid exhibits a cyclic structure, which is, maintained via an intramolecular hydrogen bond. This is reminiscent of, other macrocyclic protein phosphatase inhibitors. The inhibitor-bound, enzyme shows very little conformational change when compared with two, other PP1 structures, except in the inhibitor-sensitive beta12-beta13 loop, region. The selectivity of okadaic acid for protein phosphatases-1 and -2A, but not PP-2B (calcineurin) may be reassessed in light of this study.
About this Structure
1JK7 is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.
Reference
Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1., Maynes JT, Bateman KS, Cherney MM, Das AK, Luu HA, Holmes CF, James MN, J Biol Chem. 2001 Nov 23;276(47):44078-82. Epub 2001 Sep 4. PMID:11535607
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