6sqc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:20, 17 October 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
====
+
==Crystal structure of complex between nuclear coactivator binding domain of CBP and [1040-1086]ACTR containing alpha-methylated Leu1055 and Leu1076==
-
<StructureSection load='6sqc' size='340' side='right'caption='[[6sqc]]' scene=''>
+
<StructureSection load='6sqc' size='340' side='right'caption='[[6sqc]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6sqc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SQC FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sqc OCA], [http://pdbe.org/6sqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sqc RCSB], [http://www.ebi.ac.uk/pdbsum/6sqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sqc ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2ML:2-METHYLLEUCINE'>2ML</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6sqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sqc OCA], [https://pdbe.org/6sqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sqc RCSB], [https://www.ebi.ac.uk/pdbsum/6sqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sqc ProSAT]</span></td></tr>
</table>
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Intrinsically disordered proteins (IDPs) constitute a large portion of "Dark Proteome" - difficult to characterize or yet to be discovered protein structures. Here we used conformationally constrained alpha-methylated amino acids to bias the conformational ensemble in the free unstructured activation domain of transcriptional coactivator ACTR. Different sites and patterns of substitutions were enabled by chemical protein synthesis and led to distinct populations of alpha-helices. A specific substitution pattern resulted in a substantially higher binding affinity to nuclear coactivator binding domain (NCBD) of CREB-binding protein, a natural binding partner of ACTR. The first X-ray structure of the modified ACTR domain - NCBD complex visualized a unique conformation of ACTR and confirmed that the key alpha-methylated amino acids are localized within alpha-helices in the bound state. This study demonstrates a strategy for characterization of individual conformational states of IDPs.
 +
 +
Conformational editing of intrinsically disordered protein by alpha-methylation.,Bauer V, Schmidtgall B, Gogl G, Dolenc J, Osz J, Nomine Y, Kostmann C, Cousido-Siah A, Mitschler A, Rochel N, Trave G, Kieffer B, Torbeev V Chem Sci. 2020 Nov 4;12(3):1080-1089. doi: 10.1039/d0sc04482b. PMID:34163874<ref>PMID:34163874</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6sqc" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
 +
*[[Nuclear receptor coactivator|Nuclear receptor coactivator]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Escherichia coli K-12]]
 +
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Z-disk]]
+
[[Category: Bauer V]]
 +
[[Category: Cousido-Siah A]]
 +
[[Category: Dolenc j]]
 +
[[Category: Gogl G]]
 +
[[Category: Kieffer B]]
 +
[[Category: Kostmann C]]
 +
[[Category: Mitschler A]]
 +
[[Category: Osz J]]
 +
[[Category: Rochel N]]
 +
[[Category: Schmidtgall B]]
 +
[[Category: Torbeev V]]
 +
[[Category: Trave G]]

Current revision

Crystal structure of complex between nuclear coactivator binding domain of CBP and [1040-1086]ACTR containing alpha-methylated Leu1055 and Leu1076

PDB ID 6sqc

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/6sqc"
Personal tools