|Entry||Database: PDB / ID: 2jm5|
|Title||Solution Structure of the RGS domain from human RGS18|
|Components||Regulator of G-protein signaling 18|
|Keywords||SIGNALING PROTEIN / Structural Genomics / Structural Genomics Consortium / SGC|
|Function / homology|
Function and homology information
regulation of G protein-coupled receptor signaling pathway / negative regulation of signal transduction / GTPase activator activity / G alpha (i) signalling events / G alpha (q) signalling events / G protein-coupled receptor signaling pathway / GTPase activity / plasma membrane / cytoplasm
Similarity search - Function
Regulator of G-protein signalling 18 / Regulator of G-protein Signalling 4; domain 1 - #10 / Regulator of G-protein Signalling 4; domain 1 / RGS, subdomain 1/3 / Regulator of G-protein Signalling 4, domain 2 / Regulator of G-protein Signalling 4; domain 2 / Regulator of G protein signaling domain / RGS, subdomain 2 / RGS domain / RGS domain profile. ...Regulator of G-protein signalling 18 / Regulator of G-protein Signalling 4; domain 1 - #10 / Regulator of G-protein Signalling 4; domain 1 / RGS, subdomain 1/3 / Regulator of G-protein Signalling 4, domain 2 / Regulator of G-protein Signalling 4; domain 2 / Regulator of G protein signaling domain / RGS, subdomain 2 / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Regulator of G-protein signaling 18
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||SOLUTION NMR / simulated annealing, molecular dynamics|
|Authors||Higman, V.A. / Leidert, M. / Bray, J. / Elkins, J. / Soundararajan, M. / Doyle, D.A. / Gileadi, C. / Phillips, C. / Schoch, G. / Yang, X. ...Higman, V.A. / Leidert, M. / Bray, J. / Elkins, J. / Soundararajan, M. / Doyle, D.A. / Gileadi, C. / Phillips, C. / Schoch, G. / Yang, X. / Brockmann, C. / Schmieder, P. / Diehl, A. / Sundstrom, M. / Arrowsmith, C. / Weigelt, J. / Edwards, A. / Oschkinat, H. / Ball, L.J. / Structural Genomics Consortium (SGC)|
Journal: Proc.Natl.Acad.Sci.Usa / Year: 2008
Title: Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits.
Authors: Soundararajan, M. / Willard, F.S. / Kimple, A.J. / Turnbull, A.P. / Ball, L.J. / Schoch, G.A. / Gileadi, C. / Fedorov, O.Y. / Dowler, E.F. / Higman, V.A. / Hutsell, S.Q. / Sundstrom, M. / ...Authors: Soundararajan, M. / Willard, F.S. / Kimple, A.J. / Turnbull, A.P. / Ball, L.J. / Schoch, G.A. / Gileadi, C. / Fedorov, O.Y. / Dowler, E.F. / Higman, V.A. / Hutsell, S.Q. / Sundstrom, M. / Doyle, D.A. / Siderovski, D.P.
|Structure viewer||Molecule: |
Downloads & links
A: Regulator of G-protein signaling 18
|#1: Protein|| |
Mass: 17786.023 Da / Num. of mol.: 1 / Fragment: RGS domain, residues 75-223
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Description: BL21 (DE3) strain enriched with genes that encode rare tRNAs
Gene: RGS18, RGS13 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) - Rosetta / References: UniProt: Q9NS28
|Experiment||Method: SOLUTION NMR|
|Sample conditions||pH: 6.0 / Pressure: ambient / Temperature: 297 K|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Relative weight: 1|
|Refinement||Method: simulated annealing, molecular dynamics / Software ordinal: 1 |
Details: NOE ASSIGNMENT WITH CYANA, REFINEMENT BY SIMULATED ANNEALING IN XPLOR-NIH USING NOE RESTRAINTS AND H-BOND RESTRAINTS FROM H/D EXCHANGE DATA. WATER-REFINEMENT BY MOLECULAR DYNAMICS IN XPLOR- ...Details: NOE ASSIGNMENT WITH CYANA, REFINEMENT BY SIMULATED ANNEALING IN XPLOR-NIH USING NOE RESTRAINTS AND H-BOND RESTRAINTS FROM H/D EXCHANGE DATA. WATER-REFINEMENT BY MOLECULAR DYNAMICS IN XPLOR-NIH. THE C-TERMINAL TAIL HAS BEEN TRUNCATED PAST RESIDUE 134 BECAUSE OF FLEXIBILITY AND LACK OF STRUCTURE IN THIS REGION. THIS IS INDICATED (A) BY A LACK OF NOE RESTRAINTS PAST RESIDUE 132 AND (B) BY 15N T1, T2 AND HETERONCULEAR NOE EXPERIMENTS RESIDUE 131 ONWARDS.
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: lowest energy / Conformers calculated total number: 200 / Conformers submitted total number: 20|
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