1ygu

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the tandem phosphatase domains of RPTP CD45 with a pTyr peptide

Structural highlights

1ygu is a 4 chain structure with sequence from Homo sapiens and Murine polyomavirus strain A2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PTPRC_HUMAN T-B+ severe combined immunodeficiency due to CD45 deficiency. The disease is caused by mutations affecting the gene represented in this entry. Disease susceptibility may be associated with variations affecting the gene represented in this entry.

Function

PTPRC_HUMAN Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

CD45 is the prototypic member of transmembrane receptor-like protein tyrosine phosphatases (RPTPs) and has essential roles in immune functions. The cytoplasmic region of CD45, like many other RPTPs, contains two homologous protein tyrosine phosphatase domains, active domain 1 (D1) and catalytically impaired domain 2 (D2). Here, we report crystal structure of the cytoplasmic D1D2 segment of human CD45 in native and phosphotyrosyl peptide-bound forms. The tertiary structures of D1 and D2 are very similar, but doubly phosphorylated CD3zeta immunoreceptor tyrosine-based activation motif peptide binds only the D1 active site. The D2 "active site" deviates from the other active sites significantly to the extent that excludes any possibility of catalytic activity. The relative orientation of D1 and D2 is very similar to that observed in leukocyte common antigen-related protein with both active sites in an open conformation and is restrained through an extensive network of hydrophobic interactions, hydrogen bonds, and salt bridges. This crystal structure is incompatible with the wedge model previously suggested for CD45 regulation.

Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45.,Nam HJ, Poy F, Saito H, Frederick CA J Exp Med. 2005 Feb 7;201(3):441-52. Epub 2005 Jan 31. PMID:15684325^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nam HJ, Poy F, Saito H, Frederick CA. Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45. J Exp Med. 2005 Feb 7;201(3):441-52. Epub 2005 Jan 31. PMID:15684325 doi:10.1084/jem.20041890

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ygu"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ygu' size='340' side='right'caption='[[1ygu]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ygu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YGU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YGU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ygu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Murine_polyomavirus_strain_A2 Murine polyomavirus strain A2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YGU FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ygr|1ygr]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRC, CD45 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1ygu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ygu OCA], [https://pdbe.org/1ygu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ygu RCSB], [https://www.ebi.ac.uk/pdbsum/1ygu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ygu ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ygu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ygu OCA], [http://pdbe.org/1ygu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ygu RCSB], [http://www.ebi.ac.uk/pdbsum/1ygu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ygu ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/PTPRC_HUMAN PTPRC_HUMAN]] T-B+ severe combined immunodeficiency due to CD45 deficiency. The disease is caused by mutations affecting the gene represented in this entry.  Disease susceptibility may be associated with variations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/PTPRC_HUMAN PTPRC_HUMAN] T-B+ severe combined immunodeficiency due to CD45 deficiency. The disease is caused by mutations affecting the gene represented in this entry.  Disease susceptibility may be associated with variations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/PTPRC_HUMAN PTPRC_HUMAN]] Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity). [[http://www.uniprot.org/uniprot/MT_POVMA MT_POVMA]] Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with host Ppp2/PP2A the Src tyrosine kinase components Src, Yes and Fyn, thereby activating their kinase activity. Activation of Shc1, Pclg1 and p85 mediate signal transduction pathways leading to cell cycle progression and cell division. MT plays also a role in regulation of early and late gene expression and in viral DNA replication.<ref>PMID:16840310</ref>
+[https://www.uniprot.org/uniprot/PTPRC_HUMAN PTPRC_HUMAN] Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 17: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yg/1ygu_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 37: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Murine polyomavirus strain A2]]
-[[Category: Frederick, C A]]
+[[Category: Frederick CA]]
-[[Category: Nam, H]]
+[[Category: Nam H]]
-[[Category: Poy, F]]
+[[Category: Poy F]]
-[[Category: Saito, H]]
+[[Category: Saito H]]
-[[Category: Cd45]]
-[[Category: Hydrolase]]
-[[Category: Phosphotyrosine]]
-[[Category: Polyoma middle t antigen]]
-[[Category: Protein tyrosine phosphatase]]
-[[Category: Rptp]]

1ygu

From Proteopedia

Current revision

Crystal structure of the tandem phosphatase domains of RPTP CD45 with a pTyr peptide

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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