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| | {{STRUCTURE_1p9i| PDB=1p9i | SCENE= }} | | {{STRUCTURE_1p9i| PDB=1p9i | SCENE= }} |
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| - | '''Coiled-coil X-ray structure at 1.17 A resolution'''
| + | ===Coiled-coil X-ray structure at 1.17 A resolution=== |
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| - | ==Overview==
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| - | We determined the 1.17 A resolution X-ray crystal structure of a hybrid peptide based on sequences from coiled-coil regions of the proteins GCN4 and cortexillin I. The peptide forms a parallel homodimeric coiled-coil, with C(alpha) backbone geometry similar to GCN4 (rmsd value 0.71 A). Three stabilizing interactions have been identified: a unique hydrogen bonding-electrostatic network not previously observed in coiled-coils, and two other hydrophobic interactions involving leucine residues at positions e and g from both g-a' and d-e' interchain interactions with the hydrophobic core. This is also the first report of the quantitative significance of these interactions. The GCN4/cortexillin hybrid surprisingly has two interchain Glu-Lys' ion pairs that form a hydrogen bonding network with the Asn residues in the core. This network, which was not observed for the reversed Lys-Glu' pair in GCN4, increases the combined stability contribution of each Glu-Lys' salt bridge across the central Asn15-Asn15' core to approximately 0.7 kcal/mole, compared to approximately 0.4 kcal mole(-1) from a Glu-Lys' salt bridge on its own. In addition to electrostatic and hydrogen bonding stabilization of the coiled-coil, individual leucine residues at positions e and g in the hybrid peptide also contribute to stability by 0.7 kcal/mole relative to alanine. These interactions are of critical importance to understanding the stability requirements for coiled-coil folding and in modulating the stability of de novo designed macromolecules containing this motif.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12824486}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12824486 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12824486}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ivaninskii, S.]] | | [[Category: Ivaninskii, S.]] |
| | [[Category: Coiled-coil]] | | [[Category: Coiled-coil]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:51:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:39:48 2008'' |
Revision as of 23:39, 28 July 2008
Template:STRUCTURE 1p9i
Coiled-coil X-ray structure at 1.17 A resolution
Template:ABSTRACT PUBMED 12824486
About this Structure
Full crystallographic information is available from OCA.
Reference
Unique stabilizing interactions identified in the two-stranded alpha-helical coiled-coil: crystal structure of a cortexillin I/GCN4 hybrid coiled-coil peptide., Lee DL, Ivaninskii S, Burkhard P, Hodges RS, Protein Sci. 2003 Jul;12(7):1395-405. PMID:12824486
Page seeded by OCA on Tue Jul 29 02:39:48 2008
