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1e6h

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A-SPECTRIN SH3 DOMAIN A11V, M25I, V44I, V58L MUTANTS

Structural highlights

1e6h is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.01Å
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 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e6h"

Categories: Gallus gallus | Large Structures | Serrano L | Vega MC

@@ Line 3: / Line 3: @@
 <StructureSection load='1e6h' size='340' side='right'caption='[[1e6h]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1e6h]] 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=1E6H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E6H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1e6h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E6H FirstGlance]. <br>
-</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]], [[1e6g|1e6g]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1e6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6h OCA], [http://pdbe.org/1e6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e6h RCSB], [http://www.ebi.ac.uk/pdbsum/1e6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e6h 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=1e6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6h OCA], [https://pdbe.org/1e6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e6h RCSB], [https://www.ebi.ac.uk/pdbsum/1e6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e6h ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SPTN1_CHICK 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.
+[https://www.uniprot.org/uniprot/SPTN1_CHICK 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Spectrin|Spectrin]]
+*[[Spectrin 3D structures|Spectrin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Serrano, L]]
+[[Category: Serrano L]]
-[[Category: Vega, M C]]
+[[Category: Vega MC]]
-[[Category: Actin-binding]]
-[[Category: Calmodulin-binding]]
-[[Category: Cytoskeleton]]
-[[Category: Sh3-domain]]

1e6h

From Proteopedia

Current revision

A-SPECTRIN SH3 DOMAIN A11V, M25I, V44I, V58L MUTANTS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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