1ckr: Difference between revisions

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-[[Image:1ckr.png|left|200px]]
-<!--
+==HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES==
-The line below this paragraph, containing "STRUCTURE_1ckr", creates the "Structure Box" on the page.
+<StructureSection load='1ckr' size='340' side='right'caption='[[1ckr]]' 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'>[[1ckr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CKR 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">Solution NMR</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=1ckr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckr OCA], [https://pdbe.org/1ckr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ckr RCSB], [https://www.ebi.ac.uk/pdbsum/1ckr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ckr ProSAT]</span></td></tr>
-{{STRUCTURE_1ckr|  PDB=1ckr  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HSP7C_RAT HSP7C_RAT] Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (By similarity).
+== 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/ck/1ckr_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=1ckr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The three-dimensional structure for the substrate-binding domain of the mammalian chaperone protein Hsc70 of the 70 kDa heat shock class (HSP70) is presented. This domain includes residues 383-540 (18 kDa) and is necessary for the binding of the chaperone with substrate proteins and peptides. The high-resolution NMR solution structure is based on 4150 experimental distance constraints leading to an average root-mean-square precision of 0.38 A for the backbone atoms and 0.76 A for all atoms in the beta-sandwich sub-domain. The protein is observed to bind residue Leu539 in its hydrophobic substrate-binding groove by intramolecular interaction. The position of a helical latch differs dramatically from what is observed in the crystal and solution structures of the homologous prokaryotic chaperone DnaK. In the Hsc70 structure, the helix lies in a hydrophobic groove and is anchored by a buried salt-bridge. Residues involved in this salt-bridge appear to be important for the allosteric functioning of the protein. A mechanism for interdomain allosteric modulation of substrate-binding is proposed. It involves large-scale movements of the helical domain, redefining the location of the hinge area that enables such motions.
-===HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES===
+High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70.,Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, Zuiderweg ER J Mol Biol. 1999 Jun 25;289(5):1387-403. PMID:10373374<ref>PMID:10373374</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_10373374}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1ckr" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 10373374 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_10373374}}
-==About this Structure==
-[[1ckr]] is a 1 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKR OCA].
 ==See Also==
-*[[Heat Shock Proteins]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:10373374</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Flynn, G C.]]
+[[Category: Flynn GC]]
-[[Category: Hu, W.]]
+[[Category: Hu W]]
-[[Category: Morshauser, R C.]]
+[[Category: Morshauser RC]]
-[[Category: Pang, Y.]]
+[[Category: Pang Y]]
-[[Category: Wang, H.]]
+[[Category: Wang H]]
-[[Category: Zuiderweg, E R.P.]]
+[[Category: Zuiderweg ERP]]
-[[Category: Hsp70]]
-[[Category: Molecular chaperone]]
-[[Category: Peptide binding]]
-[[Category: Protein folding]]