1dfj | pdb_00001dfj

RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A

spinqualitylabelsall models 1dfj, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dfj is a 2 chain structure with sequence from Bos taurus and Sus scrofa. The September 2008 RCSB PDB Molecule of the Month feature on Ribonuclease A by David Goodsell is 10.2210/rcsb_pdb/mom_2008_9. The November 2011 RCSB PDB Molecule of the Month feature on Toll-like Receptors by David Goodsell is 10.2210/rcsb_pdb/mom_2011_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: ACE Activity: Pancreatic ribonuclease, with EC number 3.1.27.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA. [RINI_PIG] Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The leucine-rich repeat is a recently characterized structural motif used in molecular recognition processes as diverse as signal transduction, cell adhesion, cell development, DNA repair and RNA processing. We present here the crystal structure at 2.5 A resolution of the complex between ribonuclease A and ribonuclease inhibitor, a protein built entirely of leucine-rich repeats. The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel beta-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs. The structure can serve as a model for the interactions of other proteins containing leucine-rich repeats with their ligands. A structural basis of the interactions between leucine-rich repeats and protein ligands.,Kobe B, Deisenhofer J Nature. 1995 Mar 9;374(6518):183-6. PMID:7877692 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RNase A Temp

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