Abstracts » Zoology and wildlife conservation

Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins

Article Abstract:

The immunomodulatory substances interferon-y induces gene expression to orchestrate a cellular response. Guanylate-binding proteins GBP1 and GBP2 are abundant antiviral proteins induced by interferon-y. The crystal structure of full-length human GBP1 has been determined to 1.8 A resolution. GBP1 seems to belong to a group of large GTP-binding proteins including Mx and dynamin.

Interferon gamma

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How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP

Article Abstract:

The unique characteristics of guanylate-binding proteins (GBPs) are discussed. It is shown that the isolated amino-terminal G domain of humanGBP retains the main enzymatic properties of the full-length protein and can cleave GDP directly.

G proteins, Properties, Binding proteins

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The 2.2 Angstroms crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue

Article Abstract:

A resolution of 2.2 Angstroms is obtained from the X-ray crystal structure of the complex between the human Ras-binding domain (RBD) of the Ras effector molecule c-Raf1 and the human Ras-related protein Rap1A in the GTP analogue (GppNHp). C-Raf1 is a serine/threonine-specific protein kinase. Considering the amino-acid residues of Rap1A, it is supposed that the interaction between Ras and Raf is like of Rap and Raf. In the Rap/RBD complex, an interaction between the residues of the two antiparallel beta-strands, beta-2 from Rap and B2 from RBD is important.

Protein kinases, Complex compounds, Coordination compounds

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