1ce9
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1ce9.jpg|left|200px]] | [[Image:1ce9.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1ce9", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_1ce9| PDB=1ce9 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER''' | '''HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1CE9 is a [[Single protein]] structure | + | 1CE9 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE9 OCA]. |
==Reference== | ==Reference== | ||
| Line 30: | Line 27: | ||
[[Category: Spek, E.]] | [[Category: Spek, E.]] | ||
[[Category: Wang, L Y.]] | [[Category: Wang, L Y.]] | ||
| - | [[Category: | + | [[Category: Coiled coil]] |
| - | [[Category: | + | [[Category: Helix capping]] |
| - | [[Category: | + | [[Category: Hydrogen bonding]] |
| - | [[Category: | + | [[Category: Leucine zipper]] |
| - | [[Category: | + | [[Category: Protein folding]] |
| - | [[Category: | + | [[Category: Thermal stability]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:37:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:37, 2 May 2008
HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER
Overview
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.
About this Structure
1CE9 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 12:37:58 2008
