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.
1scm
From Proteopedia
(New page: 200px<br /><applet load="1scm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1scm, resolution 2.8Å" /> '''STRUCTURE OF THE REGU...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1scm.gif|left|200px]]<br /><applet load="1scm" size=" | + | [[Image:1scm.gif|left|200px]]<br /><applet load="1scm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1scm, resolution 2.8Å" /> | caption="1scm, resolution 2.8Å" /> | ||
'''STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The regulatory domain of scallop myosin is a three-chain protein complex | + | The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule. |
==About this Structure== | ==About this Structure== | ||
| - | 1SCM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1SCM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCM OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 18: | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:11 2008'' |
Revision as of 13:00, 21 February 2008
|
STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION
Overview
The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.
About this Structure
1SCM is a Protein complex structure of sequences from Argopecten irradians with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the regulatory domain of scallop myosin at 2.8 A resolution., Xie X, Harrison DH, Schlichting I, Sweet RM, Kalabokis VN, Szent-Gyorgyi AG, Cohen C, Nature. 1994 Mar 24;368(6469):306-12. PMID:8127365
Page seeded by OCA on Thu Feb 21 15:00:11 2008
