Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2007 Aug 28;35(17):5898–5912. doi: 10.1093/nar/gkm607

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2007 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 1. — (A) Ribbon representation of the ScRad9[754–947] 3D structure. Only fragment 762–896 is displayed. Assigned regions are in green, unassigned regions are in purple. The β-sheets are colored in magenta, except the strand β0′ which is in cyan. (B) Superimposition of the 3D structures of ScRad9[754–947] (magenta) and Crb2[358–507] (cyan). (C) Superimposition of the 3D structures of ScRad9[754–947] (magenta) and Mm53BP1[1463–1617] (yellow). (D) Ribbon representation of the 3D structure of the Rad9 fragment 762–896, calculated with three additional hydrogen bond restraints deduced from the structural comparison with Crb2 (see text). Colors are the same as in (A). (E) Alignment of the Rad9 sequence 778–896 with sequences of analogous proteins from 17 yeast species and 9 metazoans. This alignment was deduced from the structural alignment of ScRad9[754–947] with human 53BP1 tandem tudor domain [PDB reference 1XNI, (16); PDB reference 2G3R, (14)], mouse 53BP1 tandem tudor domain [PDB reference 1SSF, (15,31)] and fission yeast Crb2 tandem tudor domain [PDB reference 2FHD, (14)]. Red/blue stars indicate Rad9 solvent-exposed/buried residues whose backbone ¹⁵N or ¹Hn NMR signals are affected by addition of a 10 mer oligonucleotide. Brown stars indicate Rad9 residues whose side chain ¹⁵N or ¹Hn NMR signals are affected by the oligonucleotide addition.

Figure 1. — (A) Ribbon representation of the ScRad9[754–947] 3D structure. Only fragment 762–896 is displayed. Assigned regions are in green, unassigned regions are in purple. The β-sheets are colored in magenta, except the strand β0′ which is in cyan. (B) Superimposition of the 3D structures of ScRad9[754–947] (magenta) and Crb2[358–507] (cyan). (C) Superimposition of the 3D structures of ScRad9[754–947] (magenta) and Mm53BP1[1463–1617] (yellow). (D) Ribbon representation of the 3D structure of the Rad9 fragment 762–896, calculated with three additional hydrogen bond restraints deduced from the structural comparison with Crb2 (see text). Colors are the same as in (A). (E) Alignment of the Rad9 sequence 778–896 with sequences of analogous proteins from 17 yeast species and 9 metazoans. This alignment was deduced from the structural alignment of ScRad9[754–947] with human 53BP1 tandem tudor domain [PDB reference 1XNI, (16); PDB reference 2G3R, (14)], mouse 53BP1 tandem tudor domain [PDB reference 1SSF, (15,31)] and fission yeast Crb2 tandem tudor domain [PDB reference 2FHD, (14)]. Red/blue stars indicate Rad9 solvent-exposed/buried residues whose backbone ¹⁵N or ¹Hn NMR signals are affected by addition of a 10 mer oligonucleotide. Brown stars indicate Rad9 residues whose side chain ¹⁵N or ¹Hn NMR signals are affected by the oligonucleotide addition.