1wit

From Proteopedia

(Difference between revisions)

Current revision

TWITCHIN IMMUNOGLOBULIN SUPERFAMILY DOMAIN (IGSF MODULE) (IG 18'), NMR, MINIMIZED AVERAGE STRUCTURE

Structural highlights

1wit is a 1 chain structure with sequence from Caenorhabditis elegans. 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

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.^[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 NMR solution structure of an immunoglobulin superfamily module of twitchin (Ig 18') has been determined and the kinetic and equilibrium folding behaviour characterised. Thirty molecular coordinates were calculated using a hybrid distance geometry-simulated annealing protocol based on 1207 distance and 48 dihedral restraints. The atomic rms distributions about the mean coordinate for the ensemble of structures is 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy atoms. The protein has a topology very similar to that of telokin and the titin Ig domains and thus it falls into the I set of the immunoglobulin superfamily. The close agreement between the predicted and observed structures of Ig 18' demonstrates clearly that the I set profile can be applied in the structure prediction of immunoglobulin-like domains of diverse modular proteins. Folding studies reveal that the protein has relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1) at physiological pH. Unfolding studies suggest that the protein has considerable kinetic stability, the half life of the unfolding is greater than 40 minutes in the absence of denaturant.

Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans.,Fong S, Hamill SJ, Proctor M, Freund SM, Benian GM, Chothia C, Bycroft M, Clarke J J Mol Biol. 1996 Dec 6;264(3):624-39. PMID:8969309^[3]

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

References

↑ Waterston RH, Thomson JN, Brenner S. Mutants with altered muscle structure of Caenorhabditis elegans. Dev Biol. 1980 Jun 15;77(2):271-302. PMID:7190524
↑ Greene DN, Garcia T, Sutton RB, Gernert KM, Benian GM, Oberhauser AF. Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains. Biophys J. 2008 Aug;95(3):1360-70. doi: 10.1529/biophysj.108.130237. Epub 2008, Apr 4. PMID:18390597 doi:http://dx.doi.org/10.1529/biophysj.108.130237
↑ Fong S, Hamill SJ, Proctor M, Freund SM, Benian GM, Chothia C, Bycroft M, Clarke J. Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 1996 Dec 6;264(3):624-39. PMID:8969309 doi:http://dx.doi.org/10.1006/jmbi.1996.0665

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/1wit"

Categories: Caenorhabditis elegans | Large Structures | Bycroft M | Fong S

@@ Line 1: / Line 1: @@
 ==TWITCHIN IMMUNOGLOBULIN SUPERFAMILY DOMAIN (IGSF MODULE) (IG 18'), NMR, MINIMIZED AVERAGE STRUCTURE==
-<StructureSection load='1wit' size='340' side='right' caption='[[1wit]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1wit' size='340' side='right'caption='[[1wit]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wit]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WIT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WIT FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wiu|1wiu]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UNC-22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=1wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wit OCA], [https://pdbe.org/1wit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wit RCSB], [https://www.ebi.ac.uk/pdbsum/1wit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wit ProSAT]</span></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=1wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wit OCA], [http://pdbe.org/1wit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wit RCSB], [http://www.ebi.ac.uk/pdbsum/1wit PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
 == 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/wi/1wit_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wi/1wit_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=1wit ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Caeel]]
+[[Category: Caenorhabditis elegans]]
-[[Category: Bycroft, M]]
+[[Category: Large Structures]]
-[[Category: Fong, S]]
+[[Category: Bycroft M]]
-[[Category: I set]]
+[[Category: Fong S]]
-[[Category: Immunoglobulin superfamily]]
-[[Category: Muscle protein]]

1wit

From Proteopedia

Current revision

TWITCHIN IMMUNOGLOBULIN SUPERFAMILY DOMAIN (IGSF MODULE) (IG 18'), NMR, MINIMIZED AVERAGE STRUCTURE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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