1avj: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1avj.png|left|200px]]
-<!--
+==CALMODULIN-TYPE TCH2 PROTEIN FROM ARABIDOPSIS, THEORETICAL MODEL==
-The line below this paragraph, containing "STRUCTURE_1avj", creates the "Structure Box" on the page.
+<StructureSection load='1avj' size='340' side='right'caption='[[1avj]]' 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'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVJ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1avj FirstGlance], [https://www.ebi.ac.uk/pdbsum/1avj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1avj ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1avj|  PDB=1avj  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Plants adapt to various stresses by developmental alterations that render them less easily damaged. Expression of the TCH2 gene of Arabidopsis is strongly induced by stimuli such as touch and wind. The gene product, TCH2, belongs to the calmodulin (CaM) family of proteins and contains four highly conserved Ca(2+)-binding EF-hands. We describe here the structure of TCH2 in the fully Ca(2+)-saturated form, constructed using comparative molecular modeling, based on the x-ray structure of paramecium CaM. Like known CaMs, the overall structure consists of two globular domains separated by a linker helix. However, the linker region has added flexibility due to the presence of 5 glycines within a span of 6 residues. In addition, TCH2 is enriched in Lys and Arg residues relative to other CaMs, suggesting a preference for targets which are more negatively charged. Finally, a pair of Cys residues in the C-terminal domain, Cys126 and Cys131, are sufficiently close in space to form a disulfide bridge. These predictions serve to direct future biochemical and structural studies with the overall aim of understanding the role of TCH2 in the cellular response of Arabidopsis to environmental stimuli.
-===CALMODULIN-TYPE TCH2 PROTEIN FROM ARABIDOPSIS, THEORETICAL MODEL===
+Comparative modeling of the three-dimensional structure of the calmodulin-related TCH2 protein from Arabidopsis.,Khan AR, Johnson KA, Braam J, James MN Proteins. 1997 Jan;27(1):144-53. PMID:9037719<ref>PMID:9037719</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_9037719}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1avj" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 9037719 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9037719}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVJ OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:9037719</ref><references group="xtra"/>
 [[Category: Braam, J]]
 [[Category: James, M N.G]]
 [[Category: Johnson, K A]]
 [[Category: Khan, A R]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:49:03 2010''