1kyc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:06, 16 August 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1kyc.png|left|200px]]
 
-
<!--
+
==CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS==
-
The line below this paragraph, containing "STRUCTURE_1kyc", creates the "Structure Box" on the page.
+
<StructureSection load='1kyc' size='340' side='right'caption='[[1kyc]], [[Resolution|resolution]] 1.45&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'>[[1kyc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KYC 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]] 1.45&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
{{STRUCTURE_1kyc| PDB=1kyc | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kyc OCA], [https://pdbe.org/1kyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kyc RCSB], [https://www.ebi.ac.uk/pdbsum/1kyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kyc ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Alpha-helical coiled coils are a common protein oligomerization motif stabilized mainly by hydrophobic interactions occurring along the coiled-coil interface. We have recently designed and solved the structure of a two-heptad repeat coiled-coil peptide that is stabilized further by a complex network of inter- and intrahelical salt-bridges in addition to the hydrophobic interactions. Here, we extend and improve the de novo design of this two heptad-repeat peptide by four newly designed peptides characterized by different types of ionic interactions. The contribution of these different types of ionic interactions to coiled-coil stability are analyzed by CD spectroscopy and analytical ultracentrifugation. We show that all peptides are highly alpha-helical and two of them are 100% dimeric under physiological conditions. Furthermore, we have solved the X-ray structure of the most stable of these peptides and the rational design principles are verified by comparing this structure to the structure of the parent peptide. We show that by combining the most favorable inter- and intrahelical salt-bridge arrangements it is possible to design coiled-coil oligomerization domains with improved stability properties.
-
===CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS===
+
Improving coiled-coil stability by optimizing ionic interactions.,Burkhard P, Ivaninskii S, Lustig A J Mol Biol. 2002 May 3;318(3):901-10. PMID:12054832<ref>PMID:12054832</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_12054832}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1kyc" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 12054832 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_12054832}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYC OCA].
+
[[Category: Synthetic construct]]
-
 
+
[[Category: Burkhard P]]
-
==Reference==
+
[[Category: Ivaninskii S]]
-
Improving coiled-coil stability by optimizing ionic interactions., Burkhard P, Ivaninskii S, Lustig A, J Mol Biol. 2002 May 3;318(3):901-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054832 12054832]
+
[[Category: Lustig A]]
-
[[Category: Burkhard, P.]]
+
-
[[Category: Ivaninskii, S.]]
+
-
[[Category: Lustig, A.]]
+
-
[[Category: Alpha-helix]]
+
-
[[Category: Coiled coil]]
+
-
[[Category: De novo design]]
+
-
[[Category: Trimer]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:17:23 2008''
+

Current revision

CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS

PDB ID 1kyc

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/1kyc"
Personal tools