PDBsum entry 1zm0

Lipid binding protein

PDB id: 1zm0

Contents

Protein chains

96 a.a. *

Waters ×163

* Residue conservation analysis

PDB id:

1zm0

Name:

Lipid binding protein

Title:

Crystal structure of the carboxyl terminal ph domain of pleckstrin to 2.1 angstroms

Structure:

Pleckstrin. Chain: a, b. Fragment: ph2 domain. Synonym: platelet p47 protein. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: plek, p47. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

2.10Å R-factor: 0.236 R-free: 0.244

Authors:

S.G.Jackson,Y.Zhang,K.Zhang,R.Summerfield,R.J.Haslam,M.S.Junop

Key ref:

S.G.Jackson et al. (2006). Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 A. Acta Crystallogr D Biol Crystallogr, 62, 324-330. PubMed id: 16510979 DOI: 10.1107/S0907444905043179

Date:

09-May-05 Release date: 28-Feb-06

Protein chains

P08567  (PLEK_HUMAN) -  Pleckstrin from Homo sapiens

Seq: 350 a.a.

Struc: 96 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1107/S0907444905043179

Acta Crystallogr D Biol Crystallogr 62:324-330 (2006)

PubMed id: 16510979

Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 A.

S.G.Jackson, Y.Zhang, X.Bao, K.Zhang, R.Summerfield, R.J.Haslam, M.S.Junop.

ABSTRACT

Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH was solved by molecular replacement and refined at 2.1 A resolution. Two molecules were observed within the asymmetric unit and it is proposed that the resulting dimer interface could contribute to the previously observed oligomerization of pleckstrin in resting platelets. Structural comparisons between the phosphoinositide-binding loops of the C-PH crystal structure and the PH domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a recently described solution structure of C-PH are presented and discussed.

Selected figure(s)

Figure 2.
Figure 2 The observed non-crystallographic C-PH dimer. The dimer interface is illustrated using a combination of ribbon and semi-transparent space-filling diagrams. A reciprocal interaction between the fifth -strand from one subunit and the -helix from the other forms the dimer interface. Subunits A and B are coloured blue and yellow, respectively.

Figure 6.
Figure 6 Stereoview of the structural comparison between the DAPP1 PH and C-PH ligand-binding pockets. DAPP1 PH is shown in gold using a combined ribbon/stick representation, while C-PH is shown in purple. Ins(1,3,4,5)P[4] observed in the DAPP1 structure is shown with C atoms in green, phosphate in orange and O atoms in red.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 324-330) copyright 2006.

Figures were selected by an automated process.