Guanylate kinase
From Proteopedia
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{{STRUCTURE_1gky| PDB=1gky | SIZE=400| SCENE= |right|CAPTION=Yeast guanylate kinase complex with GMP (stick model), sulfate and acetyl group [[1gky]] }} | {{STRUCTURE_1gky| PDB=1gky | SIZE=400| SCENE= |right|CAPTION=Yeast guanylate kinase complex with GMP (stick model), sulfate and acetyl group [[1gky]] }} | ||
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| - | + | '''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<ref>PMID:8528769</ref>. 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<ref>PMID:21990344</ref>. 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. | |
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| - | '''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. 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 to a GK domain. The GK domain has no catalytic activity. The MAGUK contain PDZ, WW, SH3 and GK domains. | + | |
==3D structures of guanylate kinase== | ==3D structures of guanylate kinase== | ||
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**[[2zaj]] - hMAGUK WW 2 domain – NMR<BR /> | **[[2zaj]] - hMAGUK WW 2 domain – NMR<BR /> | ||
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| + | == References == | ||
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 12:12, 17 March 2016
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
- ↑ 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
- ↑ 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
