3sr9: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of mouse PTPsigma== | ==Crystal structure of mouse PTPsigma== | ||
<StructureSection load='3sr9' size='340' side='right' caption='[[3sr9]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3sr9' size='340' side='right'caption='[[3sr9]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sr9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3sr9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SR9 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sr9 OCA], [https://pdbe.org/3sr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sr9 RCSB], [https://www.ebi.ac.uk/pdbsum/3sr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sr9 ProSAT]</span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<table> | == Function == | ||
[https://www.uniprot.org/uniprot/PTPRS_MOUSE PTPRS_MOUSE] Interacts with LAR-interacting protein LIP.1 (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 13: | Line 15: | ||
Structural insights into the homology and differences between mouse protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-sigma.,Hou L, Wang J, Zhou Y, Li J, Zang Y, Li J Acta Biochim Biophys Sin (Shanghai). 2011 Dec;43(12):977-88. Epub 2011 Oct 25. PMID:22027896<ref>PMID:22027896</ref> | Structural insights into the homology and differences between mouse protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-sigma.,Hou L, Wang J, Zhou Y, Li J, Zang Y, Li J Acta Biochim Biophys Sin (Shanghai). 2011 Dec;43(12):977-88. Epub 2011 Oct 25. PMID:22027896<ref>PMID:22027896</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3sr9" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Tyrosine phosphatase|Tyrosine phosphatase]] | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Ding J]] | |||
[[Category: Ding | [[Category: Hou L]] | ||
[[Category: Hou | [[Category: Li J]] | ||
[[Category: Li | [[Category: Wang J]] | ||
[[Category: Wang | |||
Latest revision as of 20:26, 1 November 2023
Crystal structure of mouse PTPsigmaCrystal structure of mouse PTPsigma
Structural highlights
FunctionPTPRS_MOUSE Interacts with LAR-interacting protein LIP.1 (By similarity). Publication Abstract from PubMedProtein tyrosine phosphatases PTP-sigma (PTPsigma) plays an important role in the development of the nervous system and nerve regeneration. Although cumulative studies about the function of PTPsigma have been reported, yet limited data have been reported about the crystal structure and in vitro activity of mouse PTPsigma. Here we report the crystal structure of mouse PTPsigma tandem phosphatase domains at 2.4 A resolution. Then we compared the crystal structure of mouse PTPsigma with human PTPsigma and found that they are very similar, superimposing with a root mean square deviation of 0.45 A for 517 equivalent Calpha atoms. But some residues in mouse PTPsigma form loops while corresponding residues in human PTPsigma form beta-sheets or alpha-helices. Furthermore, we also compared in vitro activities of mouse PTPsigma with human PTPsigma and found that mouse PTPsigma has 25-fold higher specific activity than human PTPsigma does toward O-methyl fluorescein phosphate (OMFP) as the substrate. However, there is no significant activity difference between the mouse and the human enzyme detected with p-nitrophenylphosphate (pNPP) as the substrate. Mouse PTPsigma and human PTPsigma have different substrate specificities toward OMFP and pNPP as substrates. This work gives clues for further study of PTPsigma. Structural insights into the homology and differences between mouse protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-sigma.,Hou L, Wang J, Zhou Y, Li J, Zang Y, Li J Acta Biochim Biophys Sin (Shanghai). 2011 Dec;43(12):977-88. Epub 2011 Oct 25. PMID:22027896[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||