2ovn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2ovn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ovn" /> '''NMR structure of the GCN4 trigger peptide'''...)
Line 4: Line 4:
==Overview==
==Overview==
-
Coiled coils have attracted considerable interest as design templates in a, wide range of applications. Successful coiled-coil design strategies, therefore require a detailed understanding of coiled-coil folding. One, common feature shared by coiled coils is the presence of a short, autonomous helical folding unit, termed "trigger sequence," that is, indispensable for folding. Detailed knowledge of trigger sequences at the, molecular level is thus key to a general understanding of coiled-coil, formation. Using a multidisciplinary approach, we identify and, characterize here the molecular determinants that specify the helical, conformation of the monomeric early folding intermediate of the GCN4, coiled coil. We demonstrate that a network of hydrogen-bonding and, electrostatic interactions stabilize the trigger-sequence helix. This, network is rearranged in the final dimeric coiled-coil structure, and its, destabilization significantly slows down GCN4 leucine zipper folding. Our, findings provide a general explanation for the molecular mechanism of, coiled-coil formation.
+
Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed "trigger sequence," that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation.
==About this Structure==
==About this Structure==
Line 12: Line 12:
Molecular basis of coiled-coil formation., Steinmetz MO, Jelesarov I, Matousek WM, Honnappa S, Jahnke W, Missimer JH, Frank S, Alexandrescu AT, Kammerer RA, Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7062-7. Epub 2007 Apr 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17438295 17438295]
Molecular basis of coiled-coil formation., Steinmetz MO, Jelesarov I, Matousek WM, Honnappa S, Jahnke W, Missimer JH, Frank S, Alexandrescu AT, Kammerer RA, Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7062-7. Epub 2007 Apr 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17438295 17438295]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Alexandrescu, A.T.]]
+
[[Category: Alexandrescu, A T.]]
-
[[Category: Matousek, W.M.]]
+
[[Category: Matousek, W M.]]
[[Category: coiled-coil]]
[[Category: coiled-coil]]
[[Category: gcn4]]
[[Category: gcn4]]
[[Category: trigger peptide]]
[[Category: trigger peptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:05:09 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:23:05 2008''

Revision as of 16:23, 21 February 2008


2ovn

Drag the structure with the mouse to rotate

NMR structure of the GCN4 trigger peptide

Overview

Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed "trigger sequence," that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation.

About this Structure

2OVN is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Molecular basis of coiled-coil formation., Steinmetz MO, Jelesarov I, Matousek WM, Honnappa S, Jahnke W, Missimer JH, Frank S, Alexandrescu AT, Kammerer RA, Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7062-7. Epub 2007 Apr 16. PMID:17438295

Page seeded by OCA on Thu Feb 21 18:23:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools