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2b3o
From Proteopedia
(New page: 200px<br /> <applet load="2b3o" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b3o, resolution 2.8Å" /> '''Crystal structure of...) |
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| - | [[Image:2b3o.gif|left|200px]]<br /> | + | [[Image:2b3o.gif|left|200px]]<br /><applet load="2b3o" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2b3o" size=" | + | |
caption="2b3o, resolution 2.8Å" /> | caption="2b3o, resolution 2.8Å" /> | ||
'''Crystal structure of human tyrosine phosphatase SHP-1'''<br /> | '''Crystal structure of human tyrosine phosphatase SHP-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SHP-1 is a cytosolic protein-tyrosine phosphatase that behaves as a | + | SHP-1 is a cytosolic protein-tyrosine phosphatase that behaves as a negative regulator in eukaryotic cellular signaling pathways. To understand its regulatory mechanism, we have determined the crystal structure of the C-terminal truncated human SHP-1 in the inactive conformation at 2.8-A resolution and refined the structure to a crystallographic R-factor of 24.0%. The three-dimensional structure shows that the ligand-free SHP-1 has an auto-inhibited conformation. Its N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, which supports that the phosphatase activity of SHP-1 is primarily regulated by the N-SH2 domain. In addition, the C-SH2 domain of SHP-1 has a different orientation from and is more flexible than that of SHP-2, which enables us to propose an enzymatic activation mechanism in which the C-SH2 domains of SHPs could be involved in searching for phosphotyrosine activators. |
==About this Structure== | ==About this Structure== | ||
| - | 2B3O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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:// | + | 2B3O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=2B3O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Song, X.]] | [[Category: Song, X.]] | ||
[[Category: Yang, J.]] | [[Category: Yang, J.]] | ||
| - | [[Category: Zhao, Z | + | [[Category: Zhao, Z J.]] |
| - | [[Category: Zhou, G | + | [[Category: Zhou, G W.]] |
[[Category: protein tyrosine phosphatase]] | [[Category: protein tyrosine phosphatase]] | ||
[[Category: shp-1]] | [[Category: shp-1]] | ||
[[Category: signaling]] | [[Category: signaling]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:49 2008'' |
Revision as of 14:33, 21 February 2008
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Crystal structure of human tyrosine phosphatase SHP-1
Overview
SHP-1 is a cytosolic protein-tyrosine phosphatase that behaves as a negative regulator in eukaryotic cellular signaling pathways. To understand its regulatory mechanism, we have determined the crystal structure of the C-terminal truncated human SHP-1 in the inactive conformation at 2.8-A resolution and refined the structure to a crystallographic R-factor of 24.0%. The three-dimensional structure shows that the ligand-free SHP-1 has an auto-inhibited conformation. Its N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, which supports that the phosphatase activity of SHP-1 is primarily regulated by the N-SH2 domain. In addition, the C-SH2 domain of SHP-1 has a different orientation from and is more flexible than that of SHP-2, which enables us to propose an enzymatic activation mechanism in which the C-SH2 domains of SHPs could be involved in searching for phosphotyrosine activators.
About this Structure
2B3O is a Single protein structure of sequence from Homo sapiens. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Crystal structure of human protein-tyrosine phosphatase SHP-1., Yang J, Liu L, He D, Song X, Liang X, Zhao ZJ, Zhou GW, J Biol Chem. 2003 Feb 21;278(8):6516-20. Epub 2002 Dec 13. PMID:12482860
Page seeded by OCA on Thu Feb 21 16:33:49 2008
