2jv9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (19:06, 29 May 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2jv9.png|left|200px]]
 
-
<!--
+
==The Solution Structure of Calponin Homology Domain from Smoothelin-like 1==
-
The line below this paragraph, containing "STRUCTURE_2jv9", creates the "Structure Box" on the page.
+
<StructureSection load='2jv9' size='340' side='right'caption='[[2jv9]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</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=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>
-
{{STRUCTURE_2jv9| PDB=2jv9 | SCENE= }}
+
</table>
 +
== Function ==
 +
[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>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/2jv9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
===The Solution Structure of Calponin Homology Domain from Smoothelin-like 1===
+
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>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_18477568}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2jv9" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 18477568 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_18477568}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
2JV9 is a 1 chain 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].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:18477568</ref><references group="xtra"/>
+
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Ishida, H.]]
+
[[Category: Ishida H]]
-
[[Category: MacDonald, J A.]]
+
[[Category: MacDonald JA]]
-
[[Category: Vogel, H J.]]
+
[[Category: Vogel HJ]]
-
[[Category: Calponin]]
+
-
[[Category: Calponin homology domain]]
+
-
[[Category: Ch-domain]]
+
-
[[Category: Protein binding]]
+
-
[[Category: Smoothelin]]
+
-
[[Category: Smoothelin-like 1]]
+
-
[[Category: Structural protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:28:13 2009''
+

Current revision

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

PDB ID 2jv9

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/2jv9"
Personal tools