1tc0: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1tc0.png|left|200px]]


<!--
==Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP==
The line below this paragraph, containing "STRUCTURE_1tc0", creates the "Structure Box" on the page.
<StructureSection load='1tc0' size='340' side='right'caption='[[1tc0]], [[Resolution|resolution]] 2.20&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'>[[1tc0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TC0 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]] 2.2&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
{{STRUCTURE_1tc0|  PDB=1tc0  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc0 OCA], [https://pdbe.org/1tc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tc0 ProSAT]</span></td></tr>
 
</table>
===Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP===
== Function ==
 
[https://www.uniprot.org/uniprot/ENPL_CANLF ENPL_CANLF] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).
 
== Evolutionary Conservation ==
<!--
[[Image:Consurf_key_small.gif|200px|right]]
The line below this paragraph, {{ABSTRACT_PUBMED_15292259}}, adds the Publication Abstract to the page
Check<jmol>
(as it appears on PubMed at http://www.pubmed.gov), where 15292259 is the PubMed ID number.
  <jmolCheckbox>
-->
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tc/1tc0_consurf.spt"</scriptWhenChecked>
{{ABSTRACT_PUBMED_15292259}}
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
[[1tc0]] is a 2 chain structure of [[Endoplasmin]] with sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TC0 OCA].  
</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=1tc0 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Endoplasmin]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:15292259</ref><references group="xtra"/>
[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
[[Category: Dollins, D E.]]
[[Category: Large Structures]]
[[Category: Gewirth, D T.]]
[[Category: Dollins DE]]
[[Category: Immormino, R M.]]
[[Category: Gewirth DT]]
[[Category: Shaffer, P L.]]
[[Category: Immormino RM]]
[[Category: Soldano, K L.]]
[[Category: Shaffer PL]]
[[Category: Walker, M A.]]
[[Category: Soldano KL]]
[[Category: Atp]]
[[Category: Walker MA]]
[[Category: Bergerat]]
[[Category: Chaperone]]
[[Category: Endoplasmic reticulum]]
[[Category: Grp94]]
[[Category: Hsp90]]

Latest revision as of 11:38, 14 February 2024

Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATPLigand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP

Structural highlights

1tc0 is a 2 chain structure with sequence from Canis lupus familiaris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENPL_CANLF Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1tc0, resolution 2.20Å

Drag the structure with the mouse to rotate

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

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1tc0&oldid=4055451"