This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1jwd
From Proteopedia
(New page: 200px<br /><applet load="1jwd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jwd" /> '''Ca2+-induced Structural Changes in Calcyclin...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1jwd.gif|left|200px]]<br /><applet load="1jwd" size=" | + | [[Image:1jwd.gif|left|200px]]<br /><applet load="1jwd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jwd" /> | caption="1jwd" /> | ||
'''Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.'''<br /> | '''Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Calcyclin is a homodimeric protein belonging to the S100 subfamily of | + | Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes. A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear solution NMR. In order to understand the Ca(2+)-induced structural changes in S100 proteins, in-depth comparative structural analyses were used to compare the apo and Ca(2+)-bound states of calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in the second EF-hand is altered, whereas the rest of the protein, including the dimer interface, remains virtually unchanged. This Ca(2+)-induced structural change is much less drastic than the "opening" of the globular EF-hand domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using homology models of calcyclin based on S100B, a binding site in calcyclin has been proposed for the N-terminal domain of annexin XI and the C-terminal domain of the neuronal calcyclin-binding protein. The structural basis for the specificity of S100 proteins is discussed in terms of the variation in sequence of critical contact residues in the common S100 target-binding site. |
==About this Structure== | ==About this Structure== | ||
| - | 1JWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http:// | + | 1JWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chazin, W | + | [[Category: Chazin, W J.]] |
[[Category: Maler, L.]] | [[Category: Maler, L.]] | ||
[[Category: Sastry, M.]] | [[Category: Sastry, M.]] | ||
| Line 21: | Line 21: | ||
[[Category: s100a6]] | [[Category: s100a6]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:31 2008'' |
Revision as of 11:27, 21 February 2008
|
Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.
Overview
Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes. A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear solution NMR. In order to understand the Ca(2+)-induced structural changes in S100 proteins, in-depth comparative structural analyses were used to compare the apo and Ca(2+)-bound states of calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in the second EF-hand is altered, whereas the rest of the protein, including the dimer interface, remains virtually unchanged. This Ca(2+)-induced structural change is much less drastic than the "opening" of the globular EF-hand domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using homology models of calcyclin based on S100B, a binding site in calcyclin has been proposed for the N-terminal domain of annexin XI and the C-terminal domain of the neuronal calcyclin-binding protein. The structural basis for the specificity of S100 proteins is discussed in terms of the variation in sequence of critical contact residues in the common S100 target-binding site.
About this Structure
1JWD is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin., Maler L, Sastry M, Chazin WJ, J Mol Biol. 2002 Mar 22;317(2):279-90. PMID:11902843
Page seeded by OCA on Thu Feb 21 13:27:31 2008
