PDBsum entry 2xl2

Transcription

PDB id

2xl2

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Contents

			Protein chains

					304 a.a. *

			Ligands

					ASP-GLU-GLU-VAL- ASP-VAL-THR-SER- VAL-ASP ×2


					GOL ×4

			Waters ×188

* Residue conservation analysis

PDB id:

2xl2

Links

Name:

Transcription

Title:

Wdr5 in complex with an rbbp5 peptide recruited to novel site

Structure:

Wd repeat-containing protein 5. Chain: a, b. Synonym: wdr5, bmp2-induced 3-kb gene protein, wd repeat-containing protein big-3. Engineered: yes. Retinoblastoma-binding protein 5. Chain: c, d. Fragment: residues 369-381. Synonym: rbbp5, rbbp-5.

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 10090

Resolution:

2.40Å

R-factor:

0.188

R-free:

0.243

Authors:

Z.Odho,S.M.Southall,J.R.Wilson

Key ref:

Z.Odho et al. (2010). Characterization of a novel WDR5-binding site that recruits RbBP5 through a conserved motif to enhance methylation of histone H3 lysine 4 by mixed lineage leukemia protein-1. J Biol Chem, 285, 32967-32976. PubMed id: 20716525

Date:

19-Jul-10

Release date:

04-Aug-10

PROCHECK

	Headers

	References

Protein chains

P61965 (WDR5_MOUSE) - WD repeat-containing protein 5 from Mus musculus

Seq: Struc:					334 a.a. 304 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	J Biol Chem 285:32967-32976 (2010)
PubMed id: 20716525

Characterization of a novel WDR5-binding site that recruits RbBP5 through a conserved motif to enhance methylation of histone H3 lysine 4 by mixed lineage leukemia protein-1.
Z.Odho, S.M.Southall, J.R.Wilson.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21220120

V.Avdic, P.Zhang, S.Lanouette, A.Groulx, V.Tremblay, J.Brunzelle, and J.F.Couture (2011).
Structural and biochemical insights into MLL1 core complex assembly.

Structure, 19, 101-108.

PDB code:

3p4f

21124902

F.Cao, Y.Chen, T.Cierpicki, Y.Liu, V.Basrur, M.Lei, and Y.Dou (2010).
An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain.

PLoS One, 5, e14102.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.