Creatine Kinase: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 9: Line 9:
== Structural highlights ==
== Structural highlights ==


<scene name='34/345515/Cv/1'>The biological asembly of mitochondrial Creatine Kinase is homooctamer</scene>. Each monomer consists of a small alpha-helical domain and a large domain containing an eight-stranded antiparallel beta-sheet flanked by seven alpha-helices. The conserved residues of the CK family form a compact cluster that covers the active site between the domains.  
<scene name='34/345515/Cv/1'>The biological asembly of mitochondrial Creatine Kinase is homooctamer</scene>. Each monomer consists of a small alpha-helical domain and a large domain containing an eight-stranded antiparallel beta-sheet flanked by seven alpha-helices. The conserved residues of the CK family form a compact cluster that covers the active site between the domains.<ref>PMID:8692275</ref>




Line 41: Line 41:
**[[1g0w]] – bCK  
**[[1g0w]] – bCK  
}}
}}
Reference: Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W Structure of mitochondrial creatine kinase. Nature. 1996 May 23;381(6580):341-5.


== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 13:14, 31 January 2016

Crystal Structure of mitochondrial Creatine Kinase complex with phosphate 1crk

Drag the structure with the mouse to rotate

3D structures of creatine kinase

Updated on 31-January-2016

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, David Canner