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1e6g

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Revision as of 08:02, 13 December 2017

A-SPECTRIN SH3 DOMAIN A11V, V23L, M25I, V53I, V58L MUTANT

Structural highlights

1e6g 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.
Ligands:
Related:	1shg, 1tuc, 1tud, 1cun, 1bk2, 1aj3, 1aey, 1e6h
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 designed de novo 13 divergent spectrin SH3 core sequences to determine their folding properties. Kinetic analysis of the variants with stability similar to that of the wild type protein shows accelerated unfolding and refolding rates compatible with a preferential stabilization of the transition state. This is most likely caused by conformational strain in the native state, as deletion of a methyl group (Ile-->Val) leads to deceleration in unfolding and increased stability (up to 2 kcal x mol(-1)). Several of these Ile-->Val mutants have negative phi(-U) values, indicating that some noncanonical phi(-U) values might result from conformational strain. Thus, producing a stable protein does not necessarily mean that the design process has been entirely successful. Strained interactions could have been introduced, and a reduction in the buried volume could result in a large increase in stability and a reduction in unfolding rates.

Conformational strain in the hydrophobic core and its implications for protein folding and design.,Ventura S, Vega MC, Lacroix E, Angrand I, Spagnolo L, Serrano L Nat Struct Biol. 2002 Jun;9(6):485-93. PMID:12006985^[1]

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

References

↑ Ventura S, Vega MC, Lacroix E, Angrand I, Spagnolo L, Serrano L. Conformational strain in the hydrophobic core and its implications for protein folding and design. Nat Struct Biol. 2002 Jun;9(6):485-93. PMID:12006985 doi:10.1038/nsb799

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/1e6g"

@@ Line 1: / Line 1: @@
 ==A-SPECTRIN SH3 DOMAIN A11V, V23L, M25I, V53I, V58L MUTANT==
 <StructureSection load='1e6g' size='340' side='right' caption='[[1e6g]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1shg|1shg]], [[1tuc|1tuc]], [[1tud|1tud]], [[1cun|1cun]], [[1bk2|1bk2]], [[1aj3|1aj3]], [[1aey|1aey]], [[1e6h|1e6h]]</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=1e6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6g OCA], [http://pdbe.org/1e6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e6g RCSB], [http://www.ebi.ac.uk/pdbsum/1e6g PDBsum]</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=1e6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6g OCA], [http://pdbe.org/1e6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e6g RCSB], [http://www.ebi.ac.uk/pdbsum/1e6g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e6g ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/1e6g_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/1e6g_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1e6g" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Spectrin|Spectrin]]
 == References ==
 <references/>

1e6g

From Proteopedia

Revision as of 08:02, 13 December 2017

A-SPECTRIN SH3 DOMAIN A11V, V23L, M25I, V53I, V58L MUTANT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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