1e6g: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1e6g.png|left|200px]]
-<!--
+==A-SPECTRIN SH3 DOMAIN A11V, V23L, M25I, V53I, V58L MUTANT==
-The line below this paragraph, containing "STRUCTURE_1e6g", creates the "Structure Box" on the page.
+<StructureSection load='1e6g' size='340' side='right'caption='[[1e6g]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1e6g]] 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=1E6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E6G FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_1e6g|  PDB=1e6g  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6g OCA], [https://pdbe.org/1e6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e6g RCSB], [https://www.ebi.ac.uk/pdbsum/1e6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e6g ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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/e6/1e6g_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/main_output.php?pdb_ID=1e6g ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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--&gt;Val) leads to deceleration in unfolding and increased stability (up to 2 kcal x mol(-1)). Several of these Ile--&gt;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.
-===A-SPECTRIN SH3 DOMAIN A11V, V23L, M25I, V53I, V58L MUTANT===
+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<ref>PMID:12006985</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12006985}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1e6g" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12006985 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_12006985}}
-==About this Structure==
-[[1e6g]] is a 1 chain structure of [[Spectrin]] with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6G OCA].
 ==See Also==
-*[[Spectrin]]
+*[[Spectrin 3D structures|Spectrin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:12006985</ref><ref group="xtra">PMID:1279434</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Serrano, L.]]
+[[Category: Large Structures]]
-[[Category: Vega, M C.]]
+[[Category: Serrano L]]
-[[Category: Actin-binding]]
+[[Category: Vega MC]]
-[[Category: Calmodulin-binding]]
-[[Category: Cytoskeleton]]
-[[Category: Sh3-domain]]