Dynamic Properties of the Guanine Nucleotide Binding Protein Subunit and Comparison of Its Guanosine Triphosphate Hydrolase Domain
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- 作者：Luciane V. Mello ; Daan M. F. van Aalten ; and John B. C. Findlay
- 刊名：Biochemistry
- 出版年：1998
- 出版时间：March 3, 1998
- 年：1998
- 卷：37
- 期：9
- 页码：3137 - 3142
- 全文大小：110K
- 年卷期：v.37,no.9(March 3, 1998)
- ISSN：1520-4995
文摘
The dynamic properties of the 
-subunit of bovine transducin(Gt) were studied usingmolecular dynamics simulations and essential dynamics analyses.The helical domain of transducin seemsto move toward the guanosine triphosphate hydrolase (GTPase) domain.Our studies suggest that thismovement is facilitated by a hinge bending motion that is centered onresidues Gly56 and Gly179 andthat this motion may be involved in GDP release and GTP hydrolysis.The dynamic properties of theGTPase domain of Gt-GDP were compared to those ofras p21 and reveal a significant degree ofsimilarity,indicating common dynamic properties for an equivalent domain in twodifferent proteins.
-subunit of bovine transducin(Gt) were studied usingmolecular dynamics simulations and essential dynamics analyses.The helical domain of transducin seemsto move toward the guanosine triphosphate hydrolase (GTPase) domain.Our studies suggest that thismovement is facilitated by a hinge bending motion that is centered onresidues Gly56 and Gly179 andthat this motion may be involved in GDP release and GTP hydrolysis.The dynamic properties of theGTPase domain of Gt-GDP were compared to those ofras p21 and reveal a significant degree ofsimilarity,indicating common dynamic properties for an equivalent domain in twodifferent proteins.