PDBsum entry 1kn3

Protein binding

PDB id: 1kn3

Contents

Protein chain

180 a.a. *

Waters ×123

* Residue conservation analysis

PDB id:

1kn3

Name:

Protein binding

Title:

Murine pebp-2 (phosphatidylethanolamine-binding protein-2)

Structure:

Phosphatidylethanolamine binding protein-2. Chain: a. Synonym: mpebp-2. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: pebp-2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.80Å R-factor: 0.213 R-free: 0.267

Authors:

P.C.Simister,M.J.Banfield,R.L.Brady

Key ref:

P.C.Simister et al. (2002). The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family. Acta Crystallogr D Biol Crystallogr, 58, 1077-1080. PubMed id: 12037323 DOI: 10.1107/S090744490200522X

Date:

18-Dec-01 Release date: 12-Jun-02

Protein chain

Q8VIN1  (PEBP2_MOUSE) -  Phosphatidylethanolamine-binding protein 2 from Mus musculus

Seq: 187 a.a.

Struc: 180 a.a.

DOI no: 10.1107/S090744490200522X

Acta Crystallogr D Biol Crystallogr 58:1077-1080 (2002)

PubMed id: 12037323

The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family.

P.C.Simister, M.J.Banfield, R.L.Brady.

ABSTRACT

Proteins from the PEBP (phosphatidylethanolamine-binding protein) family have been identified in a wide variety of species and are thought to regulate a range of intracellular signalling cascades. The rat homologue (known as RKIP; Raf-1 kinase inhibitor protein) has been shown to negatively regulate the MAP kinase pathway through formation of inhibitory complexes with Raf-1 and MEK. The crystal structure of a new, murine member of the PEBP family, termed mPEBP-2, has been determined. On the basis of amino-acid homology, mPEBP-2 belongs to a distinct subset of the mammalian PEBP proteins. Nonetheless, mPEBP-2 is seen to be very similar in structure to other PEBP proteins from human, bovine and plant sources. Regions of distinctive sequence associated with the PEBP-2 subset are discussed with reference to this structure.

Selected figure(s)

Figure 2.
Figure 2 Stereoviews showing overlays of the mPEBP-2 and hPEBP-1 structures. (a) C^ trace showing an overlay of the mPEBP-2 and hPEBP-1 structures. The first 41 residues are coloured orange (mPEBP-2) and green (hPEBP-1), highlighting the surface region where the greatest sequence differences in the mammalian PEBP family are clustered. The rest of the C^ trace is coloured cyan (mPEBP-2) and purple (hPEBP-1). The ligand-binding site is identified by the bound cacodylate ion shown in CPK (from the hPEBP-1 structure). (b) Amino acids in the ligand-binding site [mPEBP-2 bonds in cyan, hPEBP-1 bonds in purple; bound cacodylate (from the hPEBP-1 structure) is also shown].

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2002, 58, 1077-1080) copyright 2002.

Figure was selected by an automated process.