1vj6: Difference between revisions
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==PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein== | ==PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein== | ||
<StructureSection load='1vj6' size='340' side='right'caption='[[1vj6 | <StructureSection load='1vj6' size='340' side='right'caption='[[1vj6]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vj6]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1vj6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VJ6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1vj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vj6 OCA], [https://pdbe.org/1vj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vj6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vj6 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PTN13_MOUSE PTN13_MOUSE] Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Vuister GW]] | |||
[[Category: Vuister | [[Category: Walma T]] | ||
[[Category: Walma | |||
Latest revision as of 16:25, 9 May 2024
PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC proteinPDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein
Structural highlights
FunctionPTN13_MOUSE Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling. 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 PubMedUnderstanding the basis of communication within protein domains is a major challenge in structural biology. We present structural and dynamical evidence for allosteric effects in a PDZ domain, PDZ2 from the tyrosine phosphatase PTP-BL, upon binding to a target peptide. The NMR structures of its free and peptide-bound states differ in the orientation of helix alpha2 with respect to the remainder of the molecule, concomitant with a readjustment of the hydrophobic core. Using an ultrafast mixing instrument, we detected a deviation from simple bimolecular kinetics for the association with peptide that is consistent with a rate-limiting conformational change in the protein (k(obs) approximately 7 x 10(3) s(-1)) and an induced-fit model. Furthermore, the binding kinetics of 15 mutants revealed that binding is regulated by long-range interactions, which can be correlated with the structural rearrangements resulting from peptide binding. The homologous protein PSD-95 PDZ3 did not display a similar ligand-induced conformational change. Demonstration of long-range interactions in a PDZ domain by NMR, kinetics, and protein engineering.,Gianni S, Walma T, Arcovito A, Calosci N, Bellelli A, Engstrom A, Travaglini-Allocatelli C, Brunori M, Jemth P, Vuister GW Structure. 2006 Dec;14(12):1801-9. PMID:17161370[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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