1xm2

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[[Image:1xm2.gif|left|200px]]
[[Image:1xm2.gif|left|200px]]
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{{Structure
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|PDB= 1xm2 |SIZE=350|CAPTION= <scene name='initialview01'>1xm2</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1xm2", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1xm2| PDB=1xm2 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xm2 OCA], [http://www.ebi.ac.uk/pdbsum/1xm2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xm2 RCSB]</span>
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'''Crystal structure of Human PRL-1'''
'''Crystal structure of Human PRL-1'''
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[[Category: Ryu, S E.]]
[[Category: Ryu, S E.]]
[[Category: Son, J H.]]
[[Category: Son, J H.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:12:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:51:30 2008''
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Revision as of 12:12, 3 May 2008

Image:1xm2.gif

Template:STRUCTURE 1xm2

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. 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 Page seeded by OCA on Sat May 3 15:12:16 2008

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