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2jv9

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

Structural highlights

2jv9 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wooldridge AA, Fortner CN, Lontay B, Akimoto T, Neppl RL, Facemire C, Datto MB, Kwon A, McCook E, Li P, Wang S, Thresher RJ, Miller SE, Perriard JC, Gavin TP, Hickner RC, Coffman TM, Somlyo AV, Yan Z, Haystead TA. Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle. J Biol Chem. 2008 Apr 25;283(17):11850-9. doi: 10.1074/jbc.M708628200. Epub 2008 , Feb 29. PMID:18310078 doi:http://dx.doi.org/10.1074/jbc.M708628200
↑ Lontay B, Bodoor K, Weitzel DH, Loiselle D, Fortner C, Lengyel S, Zheng D, Devente J, Hickner R, Haystead TA. Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy. J Biol Chem. 2010 Sep 17;285(38):29357-66. doi: 10.1074/jbc.M110.143966. Epub, 2010 Jul 15. PMID:20634291 doi:http://dx.doi.org/10.1074/jbc.M110.143966
↑ Ishida H, Borman MA, Ostrander J, Vogel HJ, MacDonald JA. 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. J Biol Chem. 2008 Jul 18;283(29):20569-78. Epub 2008 May 12. PMID:18477568 doi:10.1074/jbc.M800627200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jv9"

Categories: Large Structures | Mus musculus | Ishida H | MacDonald JA | Vogel HJ

@@ Line 1: / Line 1: @@
 ==The Solution Structure of Calponin Homology Domain from Smoothelin-like 1==
-<StructureSection load='2jv9' size='340' side='right' caption='[[2jv9]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
+<StructureSection load='2jv9' size='340' side='right'caption='[[2jv9]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jv9]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JV9 FirstGlance]. <br>
+<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>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Smtnl1, RP23-399J8.5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jv9 OCA], [http://pdbe.org/2jv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jv9 RCSB], [http://www.ebi.ac.uk/pdbsum/2jv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jv9 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=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>
 </table>
 == Function ==
-[[http://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>
+[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]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[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]]

2jv9

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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