2jv4 | pdb_00002jv4

Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1

spinqualitylabelsall models 2jv4, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jv4 is a 1 chain structure with sequence from A. nidulans. This structure supersedes the now removed PDB entry 2jm7. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: pinA (A. nidulans) Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 NMR solution structure of the PinA WW domain from Aspergillus nidulans is presented. The backbone of the PinA WW domain is composed of a triple-stranded anti-parallel beta-sheet and an alpha-helix similar to Ess1 and Pin1 without the alpha-helix linker. Large RMS deviations in Loop I were observed both from the NMR structures and molecular dynamics simulation suggest that the Loop I of PinA WW domain is flexible and solvent accessible, thus enabling it to bind the pS/pT-P motif. The WW domain in this structure are stabilised by a hydrophobic core. It is shown that the linker flexibility of PinA is restricted because of an alpha-helical structure in the linker region. The combination of NMR structural data and detailed Molecular Dynamics simulations enables a comprehensive structural and dynamic understanding of this protein. Structural characterisation of PinA WW domain and a comparison with other group IV WW domains, Pin1 and Ess1.,Ng CA, Kato Y, Tanokura M, Brownlee RT Biochim Biophys Acta. 2008 Sep;1784(9):1208-14. Epub 2008 May 8. PMID:18503784 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Peptidyl-prolyl cis-trans isomerase

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