1uue: Difference between revisions

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-[[Image:1uue.png|left|200px]]
-<!--
+==a-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)==
-The line below this paragraph, containing "STRUCTURE_1uue", creates the "Structure Box" on the page.
+<StructureSection load='1uue' size='340' side='right'caption='[[1uue]], [[Resolution|resolution]] 2.60&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'>[[1uue]] 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=1UUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UUE 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]] 2.6&#8491;</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=1uue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uue OCA], [https://pdbe.org/1uue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uue RCSB], [https://www.ebi.ac.uk/pdbsum/1uue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uue ProSAT]</span></td></tr>
-{{STRUCTURE_1uue|  PDB=1uue  |  SCENE=  }}
+</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/uu/1uue_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=1uue ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+An effort to combine theoretical analyses and protein engineering methods has been made to probe the folding mechanism of SH3 by using Energy Landscape Theory and a phi-value analysis. Particular emphasis was given to core residues and the effect of desolvation during the folding event by replacing the core valines with isosteric threonines. These mutations have the advantage of keeping the core structurally invariant while affecting core stability relative to the unfolded state. Although the valines that form the core appear spatially invariant, the folding kinetics of their threonine mutants varies, indicating their different extent of solvation in the transition-state ensemble. Theoretical studies predicted the distribution of folding kinetics of threonine mutants without previous knowledge of the measured rates. This initial success encourages further investigations of the molecular details behind these macroscopic phenomena and of the role of solvation in the folding mechanism.
-===A-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)===
+Solvation in protein folding analysis: combination of theoretical and experimental approaches.,Fernandez-Escamilla AM, Cheung MS, Vega MC, Wilmanns M, Onuchic JN, Serrano L Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2834-9. Epub 2004 Feb 20. PMID:14978284<ref>PMID:14978284</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_14978284}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1uue" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 14978284 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_14978284}}
-==About this Structure==
-[[1uue]] 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=1UUE OCA].
 ==See Also==
-*[[Spectrin]]
+*[[Spectrin 3D structures|Spectrin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:14978284</ref><ref group="xtra">PMID:1279434</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Fernandez, A.]]
+[[Category: Large Structures]]
-[[Category: Serrano, L.]]
+[[Category: Fernandez A]]
-[[Category: Vega, M C.]]
+[[Category: Serrano L]]
-[[Category: Wilmanns, M.]]
+[[Category: Vega MC]]
-[[Category: Actin-binding]]
+[[Category: Wilmanns M]]
-[[Category: Calcium-binding]]
-[[Category: Calmodulin-binding]]
-[[Category: Cytoskeleton]]
-[[Category: Membrane]]
-[[Category: Sh3]]
-[[Category: Sh3-domain]]
-[[Category: Spectrin]]