1ce9
From Proteopedia
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| - | [[Image:1ce9.jpg|left|200px]] | + | [[Image:1ce9.jpg|left|200px]] |
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| - | '''HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER''' | + | {{Structure |
| + | |PDB= 1ce9 |SIZE=350|CAPTION= <scene name='initialview01'>1ce9</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CE9 is a [ | + | 1CE9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10329176 10329176] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ji, H.]] | [[Category: Ji, H.]] | ||
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[[Category: thermal stability]] | [[Category: thermal stability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:16 2008'' |
Revision as of 08:23, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 of sequence from [1]. 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
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