2apq

Crystal Structure of an Active Site Mutant of Bovine Pancreatic Ribonuclease A (H119A-RNase A) with a 10-Glutamine expansion in the C-terminal hinge-loop.

spinqualitylabelsall models 2apq, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2apq is a 1 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Related: 1fs3 Gene: RNASE1, RNS1 (BOVIN) 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. 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 Amyloid or amyloid-like fibrils are elongated, insoluble protein aggregates, formed in vivo in association with neurodegenerative diseases or in vitro from soluble native proteins, respectively. The underlying structure of the fibrillar or 'cross-beta' state has presented long-standing, fundamental puzzles of protein structure. These include whether fibril-forming proteins have two structurally distinct stable states, native and fibrillar, and whether all or only part of the native protein refolds as it converts to the fibrillar state. Here we show that a designed amyloid-like fibril of the well-characterized enzyme RNase A contains native-like molecules capable of enzymatic activity. In addition, these functional molecular units are formed from a core RNase A domain and a swapped complementary domain. These findings are consistent with the zipper-spine model in which a cross-beta spine is decorated with three-dimensional domain-swapped functional units, retaining native-like structure. Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.,Sambashivan S, Liu Y, Sawaya MR, Gingery M, Eisenberg D Nature. 2005 Sep 8;437(7056):266-9. PMID:16148936 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease 3D structures

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