Crystal structure of bovine angiogenin at 1.5-A resolution.
The capacity of angiogenin ( Ang) to induce blood vessel growth is critically dependent on its ribonucleolytic activity. Crystallography and mutagenesis of human Ang have previously shown that its pyrimidine binding site is obstructed by Gln-117, implying that a conformational change is a key part of the mechanism of Ang action. The 1.5-A-resolution crystal structure of bovine Ang, in which glutamic acid is substituted for Gln-117, now confirms that a blocked active site is characteristic of these proteins. Indeed, the inactive conformation of bovine Ang is stabilized by a more extensive set of interactions than is that of human Ang. The three-dimensional structure of the putative receptor binding site is also well conserved in the two proteins. The Arg-Gly-Asp segment of this site in bovine Ang, which is replaced by Arg-Glu-Asn in human Ang, does not have a conformation typical of an integrin recognition site.[1]References
- Crystal structure of bovine angiogenin at 1.5-A resolution. Acharya, K.R., Shapiro, R., Riordan, J.F., Vallee, B.L. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
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