PDBsum entry 4eoz

Protein binding

PDB id

4eoz

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Contents

			Protein chains

					114 a.a.


					302 a.a.

			Waters ×46

PDB id:

4eoz

Links

Name:

Protein binding

Title:

Crystal structure of the spop btb domain complexed with the cul3 n- terminal domain

Structure:

Speckle-type poz protein. Chain: a, c. Fragment: btb domain from spop, unp residues 177-319. Synonym: hib homolog 1, roadkill homolog 1. Engineered: yes. Cullin-3. Chain: b, d. Fragment: n-terminal domain from cul3, unp residue 20-381. Synonym: cul-3.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: spop. Expressed in: escherichia coli. Expression_system_taxid: 511693. Gene: cul3, kiaa0617.

Resolution:

2.40Å

R-factor:

0.214

R-free:

0.263

Authors:

G.G.Prive,W.J.Errington

Key ref:

W.J.Errington et al. (2012). Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase. Structure, 20, 1141-1153. PubMed id: 22632832

Date:

16-Apr-12

Release date:

30-May-12

PROCHECK

	Headers

	References

Protein chains

O43791 (SPOP_HUMAN) - Speckle-type POZ protein from Homo sapiens

Seq: Struc:					374 a.a. 114 a.a.

Protein chains

Q13618 (CUL3_HUMAN) - Cullin-3 from Homo sapiens

Seq: Struc:

Seq: Struc:					768 a.a. 302 a.a.

Key:

Secondary structure

CATH domain

	Structure 20:1141-1153 (2012)
PubMed id: 22632832

Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase.
W.J.Errington, M.Q.Khan, S.A.Bueler, J.L.Rubinstein, A.Chakrabartty, G.G.Privé.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

23086144

R.Mathew, M.P.Seiler, S.T.Scanlon, A.P.Mao, M.G.Constantinides, C.Bertozzi-Villa, J.D.Singer, and A.Bendelac (2012).
BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.

Nature, 491, 618-621.

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.