1vhr: Difference between revisions

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[[Image:1vhr.~~gif~~|left|200px]]

[[Image:1vhr.png|left|200px]]

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~~'''~~HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE~~'''~~

===HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE===

~~==Overview==~~

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~~Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control~~ the ~~cell cycle. Here,~~ the ~~crystal structure of a human DSP, vaccinia H1-related phosphatase~~ (~~or VHR), was determined~~ at 2.~~1 angstrom resolution~~. ~~A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs~~) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region," connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the ~~PTPs, and other DSPs~~.

The line below this paragraph, {{ABSTRACT_PUBMED_8650541}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8650541 is the PubMed ID number.

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==About this Structure==

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[[Category: Hydrolase]]

[[Category: Protein dual-specificity phosphatase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 12~~:33:00 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:05:25 2008''

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-[[Image:1vhr.gif|left|200px]]
+{{Seed}}
+[[Image:1vhr.png|left|200px]]
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 {{STRUCTURE_1vhr|  PDB=1vhr  |  SCENE=  }}
-'''HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE'''
+===HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE===
-==Overview==
+<!--
-Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. Here, the crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), was determined at 2.1 angstrom resolution. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region," connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the PTPs, and other DSPs.
+The line below this paragraph, {{ABSTRACT_PUBMED_8650541}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8650541 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8650541}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Hydrolase]]
 [[Category: Protein dual-specificity phosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:33:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:05:25 2008''