|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6kip' size='340' side='right'caption='[[6kip]], [[Resolution|resolution]] 1.91Å' scene=''> | | <StructureSection load='6kip' size='340' side='right'caption='[[6kip]], [[Resolution|resolution]] 1.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6kip]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KIP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6kip]] is a 2 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=6KIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KIP FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.911Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6kip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kip OCA], [http://pdbe.org/6kip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kip RCSB], [http://www.ebi.ac.uk/pdbsum/6kip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kip ProSAT]</span></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=6kip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kip OCA], [https://pdbe.org/6kip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kip RCSB], [https://www.ebi.ac.uk/pdbsum/6kip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kip ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LIPA3_MOUSE LIPA3_MOUSE]] May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates (By similarity). | + | [https://www.uniprot.org/uniprot/PTPRD_MOUSE PTPRD_MOUSE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6kip" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6kip" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 23: |
Line 26: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-tyrosine-phosphatase]] | + | [[Category: Mus musculus]] |
| - | [[Category: Fukai, S]] | + | [[Category: Fukai S]] |
| - | [[Category: Wakita, M]] | + | [[Category: Wakita M]] |
| - | [[Category: Yamagata, A]] | + | [[Category: Yamagata A]] |
| - | [[Category: Hydrolase-protein binding complex]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein tyrosine phosphatase]]
| + | |
| - | [[Category: Sam]]
| + | |
| - | [[Category: Synapse]]
| + | |
| Structural highlights
Function
PTPRD_MOUSE
Publication Abstract from PubMed
Synapse formation is induced by transsynaptic interaction of neuronal cell-adhesion molecules termed synaptic organizers. Type IIa receptor protein tyrosine phosphatases (IIa RPTPs) function as presynaptic organizers. The cytoplasmic domain of IIa RPTPs consists of two phosphatase domains, and the membrane-distal one (D2) is essential for synapse formation. Liprin-alpha, which is an active zone protein critical for synapse formation, interacts with D2 via its C-terminal domain composed of three tandem sterile alpha motifs (tSAM). Structural mechanisms of this critical interaction for synapse formation remain elusive. Here, we report the crystal structure of the complex between mouse PTPdelta D2 and Liprin-alpha3 tSAM at 1.91 A resolution. PTPdelta D2 interacts with the N-terminal helix and the first and second SAMs (SAM1 and SAM2, respectively) of Liprin-alpha3. Structure-based mutational analyses in vitro and in cellulo demonstrate that the interactions with Liprin-alpha SAM1 and SAM2 are essential for the binding and synaptogenic activity.
Structural insights into selective interaction between type IIa receptor protein tyrosine phosphatases and Liprin-alpha.,Wakita M, Yamagata A, Shiroshima T, Izumi H, Maeda A, Sendo M, Imai A, Kubota K, Goto-Ito S, Sato Y, Mori H, Yoshida T, Fukai S Nat Commun. 2020 Jan 31;11(1):649. doi: 10.1038/s41467-020-14516-5. PMID:32005855[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wakita M, Yamagata A, Shiroshima T, Izumi H, Maeda A, Sendo M, Imai A, Kubota K, Goto-Ito S, Sato Y, Mori H, Yoshida T, Fukai S. Structural insights into selective interaction between type IIa receptor protein tyrosine phosphatases and Liprin-alpha. Nat Commun. 2020 Jan 31;11(1):649. doi: 10.1038/s41467-020-14516-5. PMID:32005855 doi:http://dx.doi.org/10.1038/s41467-020-14516-5
|
