PDBsum entry 1dro

Cytoskeleton

PDB id: 1dro

Contents

Protein chain

122 a.a. *

* Residue conservation analysis

PDB id:

1dro

Name:

Cytoskeleton

Title:

Nmr structure of the cytoskeleton/signal transduction protein

Structure:

Beta-spectrin. Chain: a. Fragment: pleckstrin homology domain. Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Organ: fruit. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: expression vector used was pgex-2t

NMR struc:

15 models

Authors:

P.Zhang,S.Talluri,H.Deng,D.Branton,G.Wagner

Key ref:

P.Zhang et al. (1995). Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin. Structure, 3, 1185-1195. PubMed id: 8591029 DOI: 10.1016/S0969-2126(01)00254-4

Date:

29-Sep-95 Release date: 03-Apr-96

Protein chain

Q00963  (SPTCB_DROME) -  Spectrin beta chain from Drosophila melanogaster

Seq: 2291 a.a.

Struc: 122 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/S0969-2126(01)00254-4

Structure 3:1185-1195 (1995)

PubMed id: 8591029

Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin.

P.Zhang, S.Talluri, H.Deng, D.Branton, G.Wagner.

ABSTRACT

BACKGROUND: The pleckstrin homology (PH) domain, which is approximately 100 amino acids long, has been found in about 70 proteins involved in signal transduction and cytoskeletal function, a frequency comparable to SH2 (src homology 2) and SH3 domains. PH domains have been shown to bind the beta gamma-subunits of G-proteins and phosphatidylinositol 4,5-bisphosphate (PIP2). It is conceivable that the PH domain of beta-spectrin plays a part in the association of spectrin with the plasma membrane of cells. RESULTS: We have solved the solution structure of the 122-residue PH domain of Drosophila beta-spectrin. The overall fold consists of two antiparallel beta-sheets packing against each other at an angle of approximately 60 degrees to form a beta-sandwich, a two-turn alpha-helix unique to spectrin PH domains, and a four-turn C-terminal alpha-helix. One of the major insertions in beta-spectrin PH domains forms a long, basic surface loop and appears to undergo slow conformational exchange in solution. This loop shows big spectral changes upon addition of D-myo-inositol 1,4,5-trisphosphate (IP3). CONCLUSIONS: We propose that the groove at the outer surface of the second beta-sheet is an important site of association with other proteins. This site and the possible lipid-binding site can serve to localize the spectrin network under the plasma membrane. More generally, it has to be considered that the common fold observed for the PH domain structures solved so far does not necessarily mean that all PH domains have similar functions. In fact, the residues constituting potential binding sites for ligands or other proteins are only slightly conserved between different PH domains.

Selected figure(s)

Figure 7.
Figure 7. A stereo view of the superposition of the 15 DspPH structures. At the top is the groove formed by the outer surface of the second β-sheet and the ill-defined β1/β2 loop and β5/β6 loop. At the right, at the open edge of the β-sandwich is the proposed PIP[2]-binding pocket. All backbone heavy atoms are shown. Figure 7. A stereo view of the superposition of the 15 DspPH structures. At the top is the groove formed by the outer surface of the second β-sheet and the ill-defined β1/β2 loop and β5/β6 loop. At the right, at the open edge of the β-sandwich is the proposed PIP[2]-binding pocket. All backbone heavy atoms are shown.

Figure 8.
Figure 8. Head-on view of the molecular surface of DspPH into the groove on the outer surface of the second β-sheet, color coded by electrostatic potential. The positive electrostatic potential is shown in blue, the negative in red, and the neutral in white. The β1/β2 loop is at the bottom, the β5/β6 loop is at the top, and in between is the groove at the outer surface of the second β-sheet. The figure was generated with the program GRASP [42]. Figure 8. Head-on view of the molecular surface of DspPH into the groove on the outer surface of the second β-sheet, color coded by electrostatic potential. The positive electrostatic potential is shown in blue, the negative in red, and the neutral in white. The β1/β2 loop is at the bottom, the β5/β6 loop is at the top, and in between is the groove at the outer surface of the second β-sheet. The figure was generated with the program GRASP [[3]42].

The above figures are reprinted by permission from Cell Press: Structure (1995, 3, 1185-1195) copyright 1995.

Figures were selected by an automated process.