1e0b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0b OCA], [http://www.ebi.ac.uk/pdbsum/1e0b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e0b RCSB]</span>
}}
}}
Line 26: Line 29:
[[Category: Mclaughlin, P J.]]
[[Category: Mclaughlin, P J.]]
[[Category: Partridge, J F.]]
[[Category: Partridge, J F.]]
-
[[Category: 1PG]]
 
[[Category: chromodomain]]
[[Category: chromodomain]]
[[Category: heterochromatin]]
[[Category: heterochromatin]]
Line 33: Line 35:
[[Category: swi6]]
[[Category: swi6]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:47:24 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:23 2008''

Revision as of 16:52, 30 March 2008


PDB ID 1e0b

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CHROMO SHADOW DOMAIN FROM FISSION YEAST SWI6 PROTEIN.


Overview

BACKGROUND: Proteins such as HP1, found in fruit flies and mammals, and Swi6, its fission yeast homologue, carry a chromodomain (CD) and a chromo shadow domain (CSD). These proteins are required to form functional transcriptionally silent centromeric chromatin, and their mutation leads to chromosome segregation defects. CSDs have only been found in tandem in proteins containing the related CD. Most HP1-interacting proteins have been found to associate through the CSD and many of these ligands contain a conserved pentapeptide motif. RESULTS: The 1.9 A crystal structure of the Swi6 CSD is presented here. This reveals a novel dimeric structure that is distinct from the previously reported monomeric nuclear magnetic resonance (NMR) structure of the CD from the mouse modifier 1 protein (MoMOD1, also known as HP1beta or M31). A prominent pit with a non-polar base is generated at the dimer interface, and is commensurate with binding an extended pentapeptide motif. Sequence alignments based on this structure highlight differences between CDs and CSDs that are superimposed on a common structural core. The analyses also revealed a previously unrecognised circumferential hydrophobic sash around the surface of the CD structure. CONCLUSIONS: Dimerisation through the CSD of HP1-like proteins results in the simultaneous formation of a putative protein-protein interaction pit, providing a potential means of targeting CSD-containing proteins to particular chromatin sites.

About this Structure

1E0B is a Single protein structure of sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.

Reference

Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis., Cowieson NP, Partridge JF, Allshire RC, McLaughlin PJ, Curr Biol. 2000 May 4;10(9):517-25. PMID:10801440

Page seeded by OCA on Sun Mar 30 19:52:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools