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1qkx

From Proteopedia

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Current revision

Alpha-spectrin Src Homology 3 domain, N47A mutant in the distal loop.

Structural highlights

1qkx 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 1.8Å
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

Residue Asn47 at position L1 of a type II' beta-turn of the alpha-spectrin SH3 domain is located in a disallowed region of the Ramachandran plot (phi = 56 +/- 12, psi = -118 +/- 17). Therefore, it is expected that replacement of Asn47 by Gly should result in a considerable stabilization of the protein. Thermodynamic analysis of the N47G and N47A mutants shows that the change in free energy is small (approximately 0.7 kcal/mol; approximately 3 kJ/mol) and comparable to that found when mutating a Gly to Ala in a alpha-helix or beta-sheet. X-ray structural analysis of these mutants shows that the conformation of the beta-turn does not change upon mutation and, therefore, that there is no relaxation of the structure, nor is there any gain or loss of interactions that could explain the small energy change. Our results indicate that the energetic definition of II' region of the Ramachandran plot (phi = 60 +/- 30, psi = -115 +/- 15) should be revised for at least Ala and Asn in structure validation and protein design.

Thermodynamic and structural characterization of Asn and Ala residues in the disallowed II' region of the Ramachandran plot.,Vega MC, Martinez JC, Serrano L Protein Sci. 2000 Dec;9(12):2322-8. PMID:11206053^[1]

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

References

↑ Vega MC, Martinez JC, Serrano L. Thermodynamic and structural characterization of Asn and Ala residues in the disallowed II' region of the Ramachandran plot. Protein Sci. 2000 Dec;9(12):2322-8. PMID:11206053

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/1qkx"

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

@@ Line 1: / Line 1: @@
-==ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, N47A MUTANT IN THE DISTAL LOOP.==
-<StructureSection load='1qkx' size='340' side='right' caption='[[1qkx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+==Alpha-spectrin Src Homology 3 domain, N47A mutant in the distal loop.==
+<StructureSection load='1qkx' size='340' side='right'caption='[[1qkx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qkx]] 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=1QKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QKX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qkx]] 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=1QKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QKX FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1shg|1shg]], [[1aey|1aey]], [[1aj3|1aj3]], [[1bk2|1bk2]], [[1cun|1cun]], [[1e6g|1e6g]], [[1e6h|1e6h]], [[1e7o|1e7o]], [[1pwt|1pwt]], [[1tuc|1tuc]], [[1tud|1tud]], [[1qkw|1qkw]]</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]] 1.8&#8491;</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=1qkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qkx OCA], [http://pdbe.org/1qkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qkx RCSB], [http://www.ebi.ac.uk/pdbsum/1qkx PDBsum]</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=1qkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qkx OCA], [https://pdbe.org/1qkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qkx RCSB], [https://www.ebi.ac.uk/pdbsum/1qkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qkx 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]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/1qkx_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/1qkx_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 ==See Also==
-*[[Spectrin|Spectrin]]
+*[[Spectrin 3D structures|Spectrin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
-[[Category: Martinez, J]]
+[[Category: Large Structures]]
-[[Category: Serrano, L]]
+[[Category: Martinez J]]
-[[Category: Vega, M C]]
+[[Category: Serrano L]]
-[[Category: Cytoskeleton]]
+[[Category: Vega MC]]
-[[Category: Membrane]]
-[[Category: Sh3 domain]]

1qkx

From Proteopedia

Current revision

Alpha-spectrin Src Homology 3 domain, N47A mutant in the distal loop.

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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