1myo

From Proteopedia

(Difference between revisions)

Current revision

SOLUTION STRUCTURE OF MYOTROPHIN, NMR, 44 STRUCTURES

Structural highlights

1myo is a 1 chain structure with sequence from Rattus norvegicus. 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

MTPN_RAT Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer (By similarity). Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy.^[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

BACKGROUND: Myotrophin is a 12.5 kDa protein that appears to have a key role in the initiation of cardiac hypertrophy, a central process in many heart diseases. Myotrophin primarily comprises ankyrin-like (ANK) repeats, the 33 amino acid motifs involved in a wide range of protein-protein interactions. As a first step in the structure-based search for cardiac hypertrophy antagonists and in order to gain insight into the molecular basis of action of the ubiquitous and multifunctional ANK repeat motif, we have determined the solution structure of myotrophin using multidimensional heteronuclear NMR spectroscopy. RESULTS: The myotrophin structure determination was based on 2786 experimental NMR restraints, and the precision of the coordinates for the final 45 simulated-annealing structures is 0.43 A for the backbone atoms and 0.87 A for all atoms. The structure of myotrophin is well defined and is ellipsoidal: approximately 46 A long and 21 A wide. The ANK repeats, which constitute the main part of the myotrophin structure, are characteristic of a hairpin-like protruding tip followed by a helix-turn-helix motif. The V-shaped helix-turn-helix of the ANK repeats stack sequentially in bundles and are stabilized by compact hydrophobic cores, whereas the protruding tips are less ordered. This arrangement is quite different to the continuous beta-sheet topology observed in the corresponding regions of another ANK protein, 53BP2, the structure of which was determined in complex with p53. CONCLUSIONS: The solution structure of myotrophin provides important insights into the structural and dynamic features of the ANK motif, and suggests that the protruding tips with highly variable sequences may be critical to facilitate diverse protein-protein recognition. The present structure also provides a molecular basis for the further functional characterization of myotrophin and the development of therapeutics for hypertrophy-related heart diseases.

The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin.,Yang Y, Nanduri S, Sen S, Qin J Structure. 1998 May 15;6(5):619-26. PMID:9634699^[3]

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

References

↑ Knuefermann P, Shi SP, Chen P, Sakata Y, Baumgarten G, Sivasubramanian N. Myotrophin/V-1 does not act as an extracellular signal to induce myocyte hypertrophy. Tex Heart Inst J. 2006;33(3):281-9. PMID:17041682
↑ Das B, Gupta S, Vasanji A, Xu Z, Misra S, Sen S. Nuclear co-translocation of myotrophin and p65 stimulates myocyte growth. Regulation by myotrophin hairpin loops. J Biol Chem. 2008 Oct 10;283(41):27947-56. doi: 10.1074/jbc.M801210200. Epub 2008, Aug 7. PMID:18693253 doi:http://dx.doi.org/10.1074/jbc.M801210200
↑ Yang Y, Nanduri S, Sen S, Qin J. The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin. Structure. 1998 May 15;6(5):619-26. PMID:9634699

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/1myo"

@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE OF MYOTROPHIN, NMR, 44 STRUCTURES==
-<StructureSection load='1myo' size='340' side='right' caption='[[1myo]], [[NMR_Ensembles_of_Models | 44 NMR models]]' scene=''>
+<StructureSection load='1myo' size='340' side='right'caption='[[1myo]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1myo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MYO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1myo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYO FirstGlance]. <br>
-</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=1myo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1myo RCSB], [http://www.ebi.ac.uk/pdbsum/1myo PDBsum]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=1myo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myo OCA], [https://pdbe.org/1myo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1myo RCSB], [https://www.ebi.ac.uk/pdbsum/1myo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1myo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MTPN_RAT MTPN_RAT]] Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer (By similarity). Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy.<ref>PMID:17041682</ref> <ref>PMID:18693253</ref>
+[https://www.uniprot.org/uniprot/MTPN_RAT MTPN_RAT] Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer (By similarity). Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy.<ref>PMID:17041682</ref> <ref>PMID:18693253</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/my/1myo_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/my/1myo_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/chain_selection.php?pdb_ID=2ata 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=1myo ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1myo" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Nanduri, S]]
+[[Category: Nanduri S]]
-[[Category: Qin, J]]
+[[Category: Qin J]]
-[[Category: Sen, S]]
+[[Category: Sen S]]
-[[Category: Yang, Y]]
+[[Category: Yang Y]]
-[[Category: Ank-repeat]]
-[[Category: Myotrophin]]

1myo

From Proteopedia

Current revision

SOLUTION STRUCTURE OF MYOTROPHIN, NMR, 44 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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