2qwq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2qwq" [edit=sysop:move=sysop])
Current revision (04:08, 2 July 2021) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2qwq.png|left|200px]]
 
-
<!--
+
==Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP hydrolyzed form==
-
The line below this paragraph, containing "STRUCTURE_2qwq", creates the "Structure Box" on the page.
+
<StructureSection load='2qwq' size='340' side='right'caption='[[2qwq]], [[Resolution|resolution]] 2.21&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'>[[2qwq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QWQ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-
-->
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qw9|2qw9]], [[2qwl|2qwl]], [[2qwm|2qwm]], [[2qwn|2qwn]], [[2qwo|2qwo]], [[2qwp|2qwp]], [[2qwr|2qwr]]</div></td></tr>
-
{{STRUCTURE_2qwq| PDB=2qwq | SCENE= }}
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA8, HSC70 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN]), DNAJC6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=2qwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qwq OCA], [https://pdbe.org/2qwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qwq RCSB], [https://www.ebi.ac.uk/pdbsum/2qwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qwq ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[https://www.uniprot.org/uniprot/HSP7C_BOVIN HSP7C_BOVIN]] 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). [[https://www.uniprot.org/uniprot/AUXI_BOVIN AUXI_BOVIN]] Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles.<ref>PMID:15502813</ref>
 +
== 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/qw/2qwq_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=2qwq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The many protein processing reactions of the ATP-hydrolyzing Hsp70s are regulated by J cochaperones, which contain J domains that stimulate Hsp70 ATPase activity and accessory domains that present protein substrates to Hsp70s. We report the structure of a J domain complexed with a J responsive portion of a mammalian Hsp70. The J domain activates ATPase activity by directing the linker that connects the Hsp70 nucleotide binding domain (NBD) and substrate binding domain (SBD) toward a hydrophobic patch on the NBD surface. Binding of the J domain to Hsp70 displaces the SBD from the NBD, which may allow the SBD flexibility to capture diverse substrates. Unlike prokaryotic Hsp70, the SBD and NBD of the mammalian chaperone interact in the ADP state. Thus, although both nucleotides and J cochaperones modulate Hsp70 NBD:linker and NBD:SBD interactions, the intrinsic persistence of those interactions differs in different Hsp70s and this may optimize their activities for different cellular roles.
-
===Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP hydrolyzed form===
+
Structural basis of J cochaperone binding and regulation of Hsp70.,Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R Mol Cell. 2007 Nov 9;28(3):422-33. PMID:17996706<ref>PMID:17996706</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_17996706}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2qwq" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 17996706 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_17996706}}
+
-
 
+
-
==About this Structure==
+
-
[[2qwq]] is a 2 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QWQ OCA].
+
==See Also==
==See Also==
-
*[[Heat Shock Proteins]]
+
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:17996706</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Bos taurus]]
+
</StructureSection>
 +
[[Category: Bovin]]
 +
[[Category: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Protein-tyrosine-phosphatase]]
-
[[Category: Hinck, A P.]]
+
[[Category: Hinck, A P]]
-
[[Category: Jiang, J.]]
+
[[Category: Jiang, J]]
-
[[Category: Lafer, E M.]]
+
[[Category: Lafer, E M]]
-
[[Category: Maes, E G.]]
+
[[Category: Maes, E G]]
-
[[Category: Sousa, R.]]
+
[[Category: Sousa, R]]
-
[[Category: Taylor, A B.]]
+
[[Category: Taylor, A B]]
-
[[Category: Wang, L.]]
+
[[Category: Wang, L]]
[[Category: Atp-binding]]
[[Category: Atp-binding]]
 +
[[Category: Chaperone]]
[[Category: Chaperone-cochaperone complex]]
[[Category: Chaperone-cochaperone complex]]
-
[[Category: Cytoplasm]]
 
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Nucleotide-binding]]
[[Category: Nucleotide-binding]]

Current revision

Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP hydrolyzed form

PDB ID 2qwq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qwq"
Personal tools