1ce9: Difference between revisions

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[[~~Image~~:1ce9.~~png|left|200px~~]]

==HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER==

== Structural highlights ==

<table><tr><td colspan='2'>[[1ce9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CE9 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ce9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ce9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ce9 PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

Capping interactions associated with specific sequences at or near the ends of alpha-helices are important determinants of the stability of protein secondary and tertiary structure. We investigate here the role of the helix-capping motif Ser-X-X-Glu, a sequence that occurs frequently at the N termini of alpha helices in proteins, on the conformation and stability of the GCN4 leucine zipper. The 1.8 A resolution crystal structure of the capped molecule reveals distinct conformations, packing geometries and hydrogen-bonding networks at the amino terminus of the two helices in the leucine zipper dimer. The free energy of helix stabilization associated with the hydrogen-bonding and hydrophobic interactions in this capping structure is -1.2 kcal/mol, evaluated from thermal unfolding experiments. A single cap thus contributes appreciably to stabilizing the terminated helix and thereby the native state. These results suggest that helix capping plays a further role in protein folding, providing a sensitive connector linking alpha-helix formation to the developing tertiary structure of a protein.

~~{{STRUCTURE_1ce9| PDB=1ce9 | SCENE= }}~~

Helix capping in the GCN4 leucine zipper.,Lu M, Shu W, Ji H, Spek E, Wang L, Kallenbach NR J Mol Biol. 1999 May 14;288(4):743-52. PMID:10329176<ref>PMID:10329176</ref>

~~===HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_10329176}}~~

==See Also==

*[[Gcn4|Gcn4]]

==~~About this Structure~~==

== References ==

[[~~1ce9~~]] ~~is a 4 chain structure. Full crystallographic information is available from [http:~~//~~oca.weizmann.ac.il/oca-bin/ocashort?id=1CE9 OCA].~~

__TOC__

</StructureSection>

[[Category: Ji, H.]]

[[Category: Kallenbach, N R.]]

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@@ Line 1: / Line 1: @@
-[[Image:1ce9.png|left|200px]]
+==HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER==
+<StructureSection load='1ce9' size='340' side='right' caption='[[1ce9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ce9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CE9 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ce9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ce9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ce9 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Capping interactions associated with specific sequences at or near the ends of alpha-helices are important determinants of the stability of protein secondary and tertiary structure. We investigate here the role of the helix-capping motif Ser-X-X-Glu, a sequence that occurs frequently at the N termini of alpha helices in proteins, on the conformation and stability of the GCN4 leucine zipper. The 1.8 A resolution crystal structure of the capped molecule reveals distinct conformations, packing geometries and hydrogen-bonding networks at the amino terminus of the two helices in the leucine zipper dimer. The free energy of helix stabilization associated with the hydrogen-bonding and hydrophobic interactions in this capping structure is -1.2 kcal/mol, evaluated from thermal unfolding experiments. A single cap thus contributes appreciably to stabilizing the terminated helix and thereby the native state. These results suggest that helix capping plays a further role in protein folding, providing a sensitive connector linking alpha-helix formation to the developing tertiary structure of a protein.
-{{STRUCTURE_1ce9|  PDB=1ce9  |  SCENE=  }}
+Helix capping in the GCN4 leucine zipper.,Lu M, Shu W, Ji H, Spek E, Wang L, Kallenbach NR J Mol Biol. 1999 May 14;288(4):743-52. PMID:10329176<ref>PMID:10329176</ref>
-===HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_10329176}}
+==See Also==
+*[[Gcn4|Gcn4]]
-==About this Structure==
+== References ==
-[[1ce9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE9 OCA].
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Ji, H.]]
 [[Category: Kallenbach, N R.]]