1wt6

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Current revision (13:34, 13 March 2024) (edit) (undo)
 
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<StructureSection load='1wt6' size='340' side='right'caption='[[1wt6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1wt6' size='340' side='right'caption='[[1wt6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1wt6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WT6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1wt6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WT6 FirstGlance]. <br>
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</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=1wt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wt6 OCA], [https://pdbe.org/1wt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1wt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wt6 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wt6 OCA], [https://pdbe.org/1wt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1wt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wt6 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/DMPK_HUMAN DMPK_HUMAN]] Defects in DMPK are the cause of dystrophia myotonica type 1 (DM1) [MIM:[https://omim.org/entry/160900 160900]]; also known as Steinert disease. A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias. Note=The causative mutation is a CTG expansion in the 3'-UTR of the DMPK gene. A length exceeding 50 CTG repeats is pathogenic, while normal individuals have 5 to 37 repeats. Intermediate alleles with 35-49 triplets are not disease-causing but show instability in intergenerational transmissions. Disease severity varies with the number of repeats: mildly affected persons have 50 to 150 repeats, patients with classic DM have 100 to 1,000 repeats, and those with congenital onset can have more than 2,000 repeats.<ref>PMID:1546326</ref> <ref>PMID:1310900</ref> <ref>PMID:1302022</ref> <ref>PMID:19514047</ref>
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[https://www.uniprot.org/uniprot/DMPK_HUMAN DMPK_HUMAN] Defects in DMPK are the cause of dystrophia myotonica type 1 (DM1) [MIM:[https://omim.org/entry/160900 160900]; also known as Steinert disease. A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias. Note=The causative mutation is a CTG expansion in the 3'-UTR of the DMPK gene. A length exceeding 50 CTG repeats is pathogenic, while normal individuals have 5 to 37 repeats. Intermediate alleles with 35-49 triplets are not disease-causing but show instability in intergenerational transmissions. Disease severity varies with the number of repeats: mildly affected persons have 50 to 150 repeats, patients with classic DM have 100 to 1,000 repeats, and those with congenital onset can have more than 2,000 repeats.<ref>PMID:1546326</ref> <ref>PMID:1310900</ref> <ref>PMID:1302022</ref> <ref>PMID:19514047</ref>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DMPK_HUMAN DMPK_HUMAN]] Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity.<ref>PMID:10913253</ref> <ref>PMID:10811636</ref> <ref>PMID:11287000</ref> <ref>PMID:15598648</ref> <ref>PMID:21457715</ref> <ref>PMID:21949239</ref>
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[https://www.uniprot.org/uniprot/DMPK_HUMAN DMPK_HUMAN] Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity.<ref>PMID:10913253</ref> <ref>PMID:10811636</ref> <ref>PMID:11287000</ref> <ref>PMID:15598648</ref> <ref>PMID:21457715</ref> <ref>PMID:21949239</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wt6 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wt6 ConSurf].
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== Publication Abstract from PubMed ==
 
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Self-assembly via coiled-coil domains (CC) is crucial for the regulation of the dystrophia myotonica kinase (DMPK) -related family of kinases. These CC domains are thought to form dimeric arrangements and thus to mediate dimerization in these enzymes. Using size exclusion chromatography combined with multiangle static light scattering, we analyzed the oligomeric state of DMPK as well as that of a truncated variant lacking the CC fraction. Remarkably, both forms were found to assemble into robust dimers. In contrast, the CC domain in isolation yielded trimeric assemblies, indicating that the oligomerization properties of CC domains from this kinase family are more diversified than anticipated. The crystal structure of this CC has been elucidated to 1.6 angstroms resolution and its properties in solution established using sedimentation equilibrium and thermal denaturation. These data show that, contrary to expectations, the self-assembly of DMPK is not dictated by the association properties of its CC domain. Instead, it appears to be driven by sequence segments flanking both N and C termini of the catalytic kinase fraction, as suggested by models of head-to-head dimers based on small angle X-ray scattering data. Our findings support a shared pattern of assembly across DMPK, ROCKs, and MRCK members of this family.
 
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Molecular insights into the self-assembly mechanism of dystrophia myotonica kinase.,Garcia P, Ucurum Z, Bucher R, Svergun DI, Huber T, Lustig A, Konarev PV, Marino M, Mayans O FASEB J. 2006 Jun;20(8):1142-51. PMID:16770013<ref>PMID:16770013</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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<div class="pdbe-citations 1wt6" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Garcia, P]]
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[[Category: Garcia P]]
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[[Category: Marino, M]]
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[[Category: Marino M]]
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[[Category: Mayans, O]]
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[[Category: Mayans O]]
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[[Category: Coiled-coil]]
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[[Category: Dmpk]]
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[[Category: Kinase activation]]
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[[Category: Molecular replacement]]
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[[Category: Transferase]]
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Current revision

Coiled-Coil domain of DMPK

PDB ID 1wt6

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OCA

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