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Human guanylate-binding protein 1
structure of human guanylate-binding protein 1 (hGBP1) in complex with the GTP-analogue GppNHp
The guanylate-binding proteins (GBPs) form a family of proteins within the Dynaminsuperfamily of large GTPases[1]. GBPs were originally found in human and murine fibroblast cells treated with interferon-α, interferon-β, or interferon-γ[2][3]. Induction with interferon-γ results in a more specific and stronger expression of the GBP [2][4]. The 67-kDa protein product of this induction has the unusual property of binding GMP, GDP, and GTP with similar affinities[2][5][6][7]. Hydrolysis of GTP by the human guanylate-binding protein 1 (hGBP1) showed that the main product of hydrolysis is GMP and GDP is only a secondary product. Furthermore, no formation of pyrophosphate during hydrolysis was detected which is explained by a consecutive hydrolysis from GTP to GDP followed by a consecutive hydrolysis of GDP to GMP[8]. While GMP is the main product of hGBP1 GTPase activity, hGBP2 showed GMP being a secondary product [9], and hGBP5 showed no detectable GMP formation [10].
^Praefcke, Gerrit J. K.; McMahon, Harvey T. (2004). "The dynamin superfamily: Universal membrane tubulation and fission molecules?". Nature Reviews Molecular Cell Biology. 5 (2): 133. doi:10.1038/nrm1313. PMID15040446.
^ abcCheng, Y. S.; Colonno, R. J.; Yin, F. H. (1983). "Interferon induction of fibroblast proteins with guanylate binding activity". The Journal of biological chemistry. 258 (12): 7746–50. PMID6305951.
^Staeheli, P; Prochazka, M; Steigmeier, P. A.; Haller, O (1984). "Genetic control of interferon action: Mouse strain distribution and inheritance of an induced protein with guanylate-binding property". Virology. 137 (1): 135–42. PMID6089411.
^Cheng, Y. S.; Becker-Manley, M. F.; Chow, T. P.; Horan, D. C. (1985). "Affinity purification of an interferon-induced human guanylate-binding protein and its characterization". The Journal of biological chemistry. 260 (29): 15834–9. PMID3934165.
^Praefcke, G. J.; Geyer, M; Schwemmle, M; Robert Kalbitzer, H; Herrmann, C (1999). "Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif". Journal of Molecular Biology. 292 (2): 321–32. doi:10.1006/jmbi.1999.3062. PMID10493878.
^Kunzelmann, S; Praefcke, G. J.; Herrmann, C (2005). "Nucleotide Binding and Self‐Stimulated GTPase Activity of Human Guanylate‐Binding Protein 1 (hGBP1)". Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1). Methods in Enzymology. Vol. 404. pp. 512–27. doi:10.1016/S0076-6879(05)04045-0. ISBN9780121828097. PMID16413296. {{cite book}}: |journal= ignored (help)
^Schwemmle, M; Staeheli, P (1994). "The interferon-induced 67-k Da guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP". The Journal of biological chemistry. 269 (15): 11299–305. PMID7512561.
^Neun, R; Richter, M. F.; Staeheli, P; Schwemmle, M (1996). "GTPase properties of the interferon-induced human guanylate-binding protein 2". FEBS letters. 390 (1): 69–72. PMID8706832.
^Wehner, M; Herrmann, C (2010). "Biochemical properties of the human guanylate binding protein 5 and a tumor-specific truncated splice variant". FEBS Journal. 277 (7): 1597–605. doi:10.1111/j.1742-4658.2010.07586.x. PMID20180847.
