1xm2
From Proteopedia
(New page: 200px<br /> <applet load="1xm2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xm2, resolution 2.7Å" /> '''Crystal structure of...) |
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| - | [[Image:1xm2.gif|left|200px]]<br /> | + | [[Image:1xm2.gif|left|200px]]<br /><applet load="1xm2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xm2" size=" | + | |
caption="1xm2, resolution 2.7Å" /> | caption="1xm2, resolution 2.7Å" /> | ||
'''Crystal structure of Human PRL-1'''<br /> | '''Crystal structure of Human PRL-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The PRL phosphatases, which constitute a subfamily of the protein tyrosine | + | The PRL phosphatases, which constitute a subfamily of the protein tyrosine phosphatases (PTPs), are implicated in oncogenic and metastatic processes. Here, we report the crystal structure of human PRL-1 determined at 2.7A resolution. The crystal structure reveals the shallow active-site pocket with highly hydrophobic character. A structural comparison with the previously determined NMR structure of PRL-3 exhibits significant differences in the active-site region. In the PRL-1 structure, a sulfate ion is bound to the active-site, providing stabilizing interactions to maintain the canonically found active conformation of PTPs, whereas the NMR structure exhibits an open conformation of the active-site. We also found that PRL-1 forms a trimer in the crystal and the trimer exists in the membrane fraction of cells, suggesting the possible biological regulation of PRL-1 activity by oligomerization. The detailed structural information on the active enzyme conformation and regulation of PRL-1 provides the structural basis for the development of potential inhibitors of PRL enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1XM2 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http:// | + | 1XM2 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XM2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jeong, D | + | [[Category: Jeong, D G.]] |
| - | [[Category: Kim, J | + | [[Category: Kim, J H.]] |
| - | [[Category: Kim, S | + | [[Category: Kim, S J.]] |
| - | [[Category: Ryu, S | + | [[Category: Ryu, S E.]] |
| - | [[Category: Son, J | + | [[Category: Son, J H.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:20 2008'' |
Revision as of 13:56, 21 February 2008
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Crystal structure of Human PRL-1
Overview
The PRL phosphatases, which constitute a subfamily of the protein tyrosine phosphatases (PTPs), are implicated in oncogenic and metastatic processes. Here, we report the crystal structure of human PRL-1 determined at 2.7A resolution. The crystal structure reveals the shallow active-site pocket with highly hydrophobic character. A structural comparison with the previously determined NMR structure of PRL-3 exhibits significant differences in the active-site region. In the PRL-1 structure, a sulfate ion is bound to the active-site, providing stabilizing interactions to maintain the canonically found active conformation of PTPs, whereas the NMR structure exhibits an open conformation of the active-site. We also found that PRL-1 forms a trimer in the crystal and the trimer exists in the membrane fraction of cells, suggesting the possible biological regulation of PRL-1 activity by oligomerization. The detailed structural information on the active enzyme conformation and regulation of PRL-1 provides the structural basis for the development of potential inhibitors of PRL enzymes.
About this Structure
1XM2 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms., Jeong DG, Kim SJ, Kim JH, Son JH, Park MR, Lim SM, Yoon TS, Ryu SE, J Mol Biol. 2005 Jan 14;345(2):401-13. PMID:15571731
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