1 / 1

401_2014_1323_MOESM2_ESM

A. B.

iria
Download Presentation

401_2014_1323_MOESM2_ESM

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript


  1. A B Supplemental Material 2: SMARCA4 protein model. View of the full SMARCA4 model (A), showing the location of Asp-779 in the ATP binding region of the ATPase domain, which was affected by a homozygous missense mutation resulting in an amino acid exchange (p.Asp779Asn) in case #9. (B) Zoom of the region around Asp-779, which is shown in ball-and-stick format (carbons light brown, oxygens red). The location of four contacting residues are also shown: Leu-783 (green stick-format, left), Leu-777 (green right), Arg-979 (tan/blue sticks in front) and Gln-788 (tan/blue/red sticks back). We obtained a model of SMARCA4 (Uniprot P51532) from the Modbase resource (PMID: 21097780) and obtained an approximate structures of bound DNA by using STAMP (PMID 1409577) to superimpose and re-orient this model onto the structure of S. solfataricusSWI2/SNF2 ATPase core in complex with dsDNA (PDB 1z63, PMID 15882619), and of bound ATP by superimposition with G. stearothermophilusPCRA (PDB 1qhh; PMID 10388562). Both of these proteins are in the wider helicase superfamily, though inspection of other bound structures (ATP analogs, shorter DNA fragments, etc.) shows the approximate locations to be accurate.

More Related