Structural highlights
Function
[KCRM_HUMAN] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of human muscle creatine kinase has been determined by the molecular-replacement method and refined at 3.5A resolution. The structures of both the monomer and the dimer closely resemble those of the other known structures in the creatine kinase family. Two types of dimers, one with a non-crystallographic twofold symmetry axis and the other with a crystallographic twofold symmetry axis, were found to exist simultaneously in the crystal. These dimers form an infinite "double-helix"-like structure along an unusual long crystallographic 3(1) axis.
Structure of human muscle creatine kinase.,Shen YQ, Tang L, Zhou HM, Lin ZJ Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1196-200. PMID:11517911[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shen YQ, Tang L, Zhou HM, Lin ZJ. Structure of human muscle creatine kinase. Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1196-200. PMID:11517911
