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1tud

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Revision as of 08:35, 21 March 2018

ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48

Structural highlights

1tud is a 1 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.

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

We have analyzed the structure, stability and folding kinetics of circularly permuted forms of alpha-spectrin SH3 domain. All the possible permutations involving the disruption of the covalent linkage between two beta-strands forming a beta-hairpin have been done. The different proteins constructed here fold to a native conformation similar to that of wild-type protein, as demonstrated by nuclear magnetic resonance and circular dichroism. Although all the mutants have similar stabilities (they are 1 to 2 kcal mol-1 less stable than the wild-type) their rate constants for folding and unfolding are quite different. Protein engineering, in combination with kinetics indicates that the folding pathway has been changed in the circularly permuted proteins. We conclude that neither the order of secondary structure elements, nor the preservation of any of the beta-hairpins present in this domain, is crucial for the ability of the polypeptide to fold, but they influence the folding and unfolding kinetics and could determine its folding pathway.

The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics.,Viguera AR, Blanco FJ, Serrano L J Mol Biol. 1995 Apr 7;247(4):670-81. PMID:7723022^[1]

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

References

↑ Viguera AR, Blanco FJ, Serrano L. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J Mol Biol. 1995 Apr 7;247(4):670-81. PMID:7723022 doi:http://dx.doi.org/10.1006/jmbi.1994.0171

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tud"

@@ Line 1: / Line 1: @@
 ==ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48==
 <StructureSection load='1tud' size='340' side='right' caption='[[1tud]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1tud]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TUD 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=1tud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tud OCA], [http://pdbe.org/1tud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tud RCSB], [http://www.ebi.ac.uk/pdbsum/1tud PDBsum]</span></td></tr>
+</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=1tud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tud OCA], [http://pdbe.org/1tud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tud RCSB], [http://www.ebi.ac.uk/pdbsum/1tud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tud ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tu/1tud_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tu/1tud_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1tud

From Proteopedia

Revision as of 08:35, 21 March 2018

ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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