3uto

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:27, 1 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3uto' size='340' side='right'caption='[[3uto]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3uto' size='340' side='right'caption='[[3uto]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3uto]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTO FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3uto]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTO FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.4&#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;'>[[1koa|1koa]], [[1kob|1kob]], [[1tki|1tki]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">unc-22, ZK617.1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3uto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uto OCA], [https://pdbe.org/3uto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uto RCSB], [https://www.ebi.ac.uk/pdbsum/3uto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uto 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=3uto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uto OCA], [https://pdbe.org/3uto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uto RCSB], [https://www.ebi.ac.uk/pdbsum/3uto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uto ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/UNC22_CAEEL UNC22_CAEEL]] Regulator of muscle contraction and relaxation. Senses mechanical strain that occurs during muscle activity by unfolding in clearly resolvable steps at differing forces.<ref>PMID:7190524</ref> <ref>PMID:18390597</ref>
+
[https://www.uniprot.org/uniprot/UNC22_CAEEL UNC22_CAEEL] Regulator of muscle contraction and relaxation. Senses mechanical strain that occurs during muscle activity by unfolding in clearly resolvable steps at differing forces.<ref>PMID:7190524</ref> <ref>PMID:18390597</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Titin-like kinases are an important class of cytoskeletal kinases that intervene in the response of muscle to mechanical stimulation, being central to myofibril homeostasis and development. These kinases exist in autoinhibited states and, allegedly, become activated during muscle activity by the elastic unfolding of a C-terminal regulatory segment (CRD). However, this mechano-activation model remains controversial. Here we explore the structural, catalytic, and tensile properties of the multidomain kinase region of Caenorhabditis elegans twitchin (Fn(31)-Nlinker-kinase-CRD-Ig(26)) using X-ray crystallography, small angle X-ray scattering, molecular dynamics simulations, and catalytic assays. This work uncovers the existence of an inhibitory segment that flanks the kinase N-terminally (N-linker) and that acts synergistically with the canonical CRD tail to silence catalysis. The N-linker region has high mechanical lability and acts as the primary stretch-sensor in twitchin kinase, while the CRD is poorly responsive to pulling forces. This poor response suggests that the CRD is not a generic mechanosensor in this kinase family. Instead, the CRD is shown here to be permissive to catalysis and might protect the kinase active site against mechanical damage. Thus, we put forward a regulatory model where kinase inhibition results from the combined action of both N- and C-terminal tails, but only the N-terminal extension undergoes mechanical removal, thereby affording partial activation. Further, we compare invertebrate and vertebrate titin-like kinases and identify variations in the regulatory segments that suggest a mechanical speciation of these kinase classes.
+
-
 
+
-
Identification of an N-terminal inhibitory extension as the primary mechanosensory regulator of twitchin kinase.,von Castelmur E, Strumpfer J, Franke B, Bogomolovas J, Barbieri S, Qadota H, Konarev PV, Svergun DI, Labeit S, Benian GM, Schulten K, Mayans O Proc Natl Acad Sci U S A. 2012 Aug 21;109(34):13608-13. Epub 2012 Aug 6. PMID:22869697<ref>PMID:22869697</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3uto" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Caeel]]
+
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Non-specific serine/threonine protein kinase]]
+
[[Category: Barbieri S]]
-
[[Category: Barbieri, S]]
+
[[Category: Castelmur E]]
-
[[Category: Castelmur, E]]
+
[[Category: Mayans O]]
-
[[Category: Mayans, O]]
+
-
[[Category: Kinase]]
+
-
[[Category: Muscle sarcomere]]
+
-
[[Category: Transferase]]
+

Current revision

Twitchin kinase region from C.elegans (Fn31-NL-kin-CRD-Ig26)

PDB ID 3uto

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3uto"
Personal tools