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| {{STRUCTURE_1xm2| PDB=1xm2 | SCENE= }} | | {{STRUCTURE_1xm2| PDB=1xm2 | SCENE= }} |
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| '''Crystal structure of Human PRL-1'''
| | ===Crystal structure of Human PRL-1=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15571731}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15571731 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15571731}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Son, J H.]] | | [[Category: Son, J H.]] |
| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:12:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:30:03 2008'' |