Mouse RI

"Mouse RI bound to mouse ribonuclease I forms a tetramer in the crystallographic asymmetric unit .The tetramer consists of two dimers that are related by a glide plane.The monomers of both dimers adopt a right handed helix whose parameters are quite similar to those in the dimer of human RI- angiogenin/ribonuclease I whose LRRs belong to the “RI-like” class, also forms a homo-dimer in the crystal and in solution. The two monomersin the LGR4 dimer are in close proximity at their C-terminal sides and are related by a twofold axis of rotation-TLRs 1-6, TLR8, RP105, LGR4,LGR5, and Drosophila Toll. 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 April, 2024