2esb
From Proteopedia
(New page: 200px<br /> <applet load="2esb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2esb, resolution 2.Å" /> '''Crystal structure of ...) |
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| - | [[Image:2esb.gif|left|200px]]<br /> | + | [[Image:2esb.gif|left|200px]]<br /><applet load="2esb" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2esb" size=" | + | |
caption="2esb, resolution 2.Å" /> | caption="2esb, resolution 2.Å" /> | ||
'''Crystal structure of human DUSP18'''<br /> | '''Crystal structure of human DUSP18'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human dual-specificity protein phosphatase 18 (DSP18) gene and its | + | The human dual-specificity protein phosphatase 18 (DSP18) gene and its protein product have recently been characterized. Like most DSPs, DSP18 displays dephosphorylating activity towards both phosphotyrosine and phosphothreonine residues. However, DSP18 is distinct from other known DSPs in terms of the existence of approximately 30 residues at the C-terminus of the catalytic domain and an unusual optimum activity profile at 328 K. The crystal structure of human DSP18 has been determined at 2.0 A resolution. The catalytic domain of DSP18 adopts a fold similar to that known for other DSP structures. Although good alignments are found with other DSPs, substantial differences are also found in the regions surrounding the active site, suggesting that DSP18 constitutes a unique structure with a distinct substrate specificity. Furthermore, the residues at the C-terminus fold into two antiparallel beta-strands and participate in extensive interactions with the catalytic domain, explaining the thermostability of DSP18. |
==About this Structure== | ==About this Structure== | ||
| - | 2ESB 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 ACT and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2ESB 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=ACT:'>ACT</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cho, Y | + | [[Category: Cho, Y H.]] |
| - | [[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: Yoon, T | + | [[Category: Yoon, T S.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: EPE]] | [[Category: EPE]] | ||
[[Category: alpha/beta structure]] | [[Category: alpha/beta structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:05 2008'' |
Revision as of 15:14, 21 February 2008
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Crystal structure of human DUSP18
Overview
The human dual-specificity protein phosphatase 18 (DSP18) gene and its protein product have recently been characterized. Like most DSPs, DSP18 displays dephosphorylating activity towards both phosphotyrosine and phosphothreonine residues. However, DSP18 is distinct from other known DSPs in terms of the existence of approximately 30 residues at the C-terminus of the catalytic domain and an unusual optimum activity profile at 328 K. The crystal structure of human DSP18 has been determined at 2.0 A resolution. The catalytic domain of DSP18 adopts a fold similar to that known for other DSP structures. Although good alignments are found with other DSPs, substantial differences are also found in the regions surrounding the active site, suggesting that DSP18 constitutes a unique structure with a distinct substrate specificity. Furthermore, the residues at the C-terminus fold into two antiparallel beta-strands and participate in extensive interactions with the catalytic domain, explaining the thermostability of DSP18.
About this Structure
2ESB is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family., Jeong DG, Cho YH, Yoon TS, Kim JH, Son JH, Ryu SE, Kim SJ, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):582-8. Epub 2006, May 12. PMID:16699184
Page seeded by OCA on Thu Feb 21 17:14:05 2008
Categories: Homo sapiens | Single protein | Cho, Y H. | Jeong, D G. | Kim, J H. | Kim, S J. | Ryu, S E. | Yoon, T S. | ACT | EPE | Alpha/beta structure
