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2jv9

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{{Seed}}
 
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[[Image:2jv9.png|left|200px]]
 
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==The Solution Structure of Calponin Homology Domain from Smoothelin-like 1==
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The line below this paragraph, containing "STRUCTURE_2jv9", creates the "Structure Box" on the page.
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<StructureSection load='2jv9' size='340' side='right'caption='[[2jv9]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jv9]] is a 1 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=2JV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JV9 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jv9 OCA], [https://pdbe.org/2jv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jv9 RCSB], [https://www.ebi.ac.uk/pdbsum/2jv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jv9 ProSAT]</span></td></tr>
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{{STRUCTURE_2jv9| PDB=2jv9 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SMTL1_MOUSE SMTL1_MOUSE] Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-301 reduces this inhibitory activity.<ref>PMID:18310078</ref> <ref>PMID:20634291</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/2jv9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2jv9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The SMTNL1 protein contains a single type-2 calponin homology (CH) domain at its C terminus that shares sequence identity with the smoothelin family of smooth muscle-specific proteins. In contrast to the smoothelins, SMTNL1 does not associate with F-actin in vitro, and its specific role in smooth muscle remains unclear. In addition, the biological function of the C-terminal CH-domains found in the smoothelin proteins is also poorly understood. In this work, we have therefore determined the solution structure of the CH-domain of mouse SMTNL1 (SMTNL1-CH; residues 346-459). The secondary structure and the overall fold for the C-terminal type-2 CH-domain is very similar to that of other CH-domains. However, two clusters of basic residues form a unique surface structure that is characteristic of SMTNL1-CH. Moreover, the protein has an extended C-terminal alpha-helix, which contains a calmodulin (CaM)-binding IQ-motif, that is also a distinct feature of the smoothelins. We have characterized the binding of apo-CaM to SMTNL1-CH through its IQ-motif by isothermal titration calorimetry and NMR chemical shift perturbation studies. In addition, we have used the HADDOCK protein-protein docking approach to construct a model for the complex of apo-CaM and SMTNL1-CH. The model revealed a close interaction of SMTNL1-CH with the two Ca(2+) binding loop regions of the C-terminal domain of apo-CaM; this mode of apo-CaM binding is distinct from previously reported interactions of apo-CaM with IQ-motifs. Finally, we comment on the putative role of the CH-domain in the biological function of SMTNL1.
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===The Solution Structure of Calponin Homology Domain from Smoothelin-like 1===
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Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation.,Ishida H, Borman MA, Ostrander J, Vogel HJ, MacDonald JA J Biol Chem. 2008 Jul 18;283(29):20569-78. Epub 2008 May 12. PMID:18477568<ref>PMID:18477568</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>
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The line below this paragraph, {{ABSTRACT_PUBMED_18477568}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2jv9" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18477568 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18477568}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2JV9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JV9 OCA].
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==Reference==
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Solution structure of the calponin homology (CH)-domain from the smoothelin-like 1 protein: a unique Apo-calmodulin binding mode and the possible role of the C-terminal type 2 CH-domain in smooth muscle relaxation., Ishida H, Borman Meredith A, Ostrander J, Vogel Hans J, Macdonald Justin A, J Biol Chem. 2008 May 12;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18477568 18477568]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Ishida H]]
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[[Category: Ishida, H.]]
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[[Category: MacDonald JA]]
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[[Category: MacDonald, J A.]]
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[[Category: Vogel HJ]]
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[[Category: Vogel, H J.]]
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[[Category: Calponin]]
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[[Category: Calponin homology domain]]
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[[Category: Ch-domain]]
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[[Category: Protein binding]]
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[[Category: Smoothelin]]
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[[Category: Smoothelin-like 1]]
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[[Category: Structural protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:41:45 2008''
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Current revision

The Solution Structure of Calponin Homology Domain from Smoothelin-like 1

PDB ID 2jv9

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