Human RI

"Human RI complexed with human angiogenin or ribonuclease I forms a dimer with human RI-angiogenin/ribonuclease I. The whole molecule of human RI consists of only LRRs; all belong to “RI- like” class. The two complexes are held together by many hydrogen bonds formed between the N-terminal ß-strands of the two human RI molecules, leading to the formation of an antiparallel lß-sheet. The entire RI dimer adopts a right handed helix whose helical parameters are similar to those of its individual monomers. These two hRI molecules are related by an approximate two fold axis of rotation, nearly perpendicular to the common helical axis. OMICS Group International is one of the leading Open Access Publishers which is publishing 700+ peer-reviewed journals with the support of 50,000+ editorial board members as editorial team and aimed to disseminate the scholarly knowledge to the scientific society. OMICS Group also organizing 3000+ International Scientific Conferences and events yearly all over the world with the support of 1000+ Scientific associations worldwide. Citation: Enkhbayar P, Miyashita H, Kretsinger RH, Matsushima N (2014) Helical Parameters and Correlations of Tandem Leucine Rich Repeats in Proteins. J Proteomics Bio inform 7: 139-150."

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Last date updated on September, 2024