Guanylate kinase

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Template:STRUCTURE 1gky


Guanylate kinase (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP[1]. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain[2]. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains.

3D structures of guanylate kinase

Updated on 17-March-2016

References

  1. ↑ White SH, Wimley WC, Selsted ME. Structure, function, and membrane integration of defensins. Curr Opin Struct Biol. 1995 Aug;5(4):521-7. PMID:8528769
  2. ↑ Johnston CA, Whitney DS, Volkman BF, Doe CQ, Prehoda KE. Conversion of the enzyme guanylate kinase into a mitotic-spindle orienting protein by a single mutation that inhibits GMP-induced closing. Proc Natl Acad Sci U S A. 2011 Nov 1;108(44):E973-8. Epub 2011 Oct 11. PMID:21990344 doi:10.1073/pnas.1104365108

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Michal Harel, Alexander Berchansky

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