PDBsum entry 1jxm

Structural protein

PDB id: 1jxm

Contents

Protein chain

264 a.a. *

Ligands

5GP

GAI ×2

MPD ×2

Waters ×87

* Residue conservation analysis

PDB id:

1jxm

Name:

Structural protein

Title:

Crystal structure of the gmp bound sh3-hook-gk fragment of psd-95

Structure:

Postsynaptic density protein. Chain: a. Fragment: sh3-hook-gk. Synonym: postsynaptic density-95, psd-95. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: brain. Gene: psd-95. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.237 R-free: 0.260

Authors:

G.A.Tavares,E.H.Panepucci,A.T.Brunger

Key ref:

G.A.Tavares et al. (2001). Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95. Mol Cell, 8, 1313-1325. PubMed id: 11779506 DOI: 10.1016/S1097-2765(01)00416-6

Date:

07-Sep-01 Release date: 16-Jan-02

Protein chain

P31016  (DLG4_RAT) -  Disks large homolog 4 from Rattus norvegicus

Seq: 724 a.a.

Struc: 264 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/S1097-2765(01)00416-6

Mol Cell 8:1313-1325 (2001)

PubMed id: 11779506

Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.

G.A.Tavares, E.H.Panepucci, A.T.Brunger.

ABSTRACT

PSD-95/SAP90 is a member of the MAGUK superfamily. In excitatory synapses, PSD-95 clusters receptors and ion channels at specific sites in the postsynaptic membrane and organizes downstream signaling and cytoskeletal molecules. We have determined the crystal structures of the apo and GMP-bound forms to 2.3 and 2.0 A resolutions, respectively, of a fragment containing the SH3, HOOK, and guanylate kinase (GK) domains of PSD-95. We observe an intramolecular interaction between the SH3 and GK domains involving the formation of a beta sheet including residues N- and C-terminal to the GK domain. Based on amino acid conservation and mutational data available in the literature, we propose that this intramolecular interaction is a common feature among MAGUK proteins.

Selected figure(s)

Figure 1.
Figure 1. PSD-95 Domain Organization and Overall Architecture of PSD-95 SH3-HOOK-GK Domains(A) PSD-95 domain organization showing the conserved core of MAGUK proteins and the fragment studied in this work (SH3-HOOK-GK).(B) SH3-HOOK-GK model built using the GMP-bound structure and residues 439–445 and 502–508 from the apo form. In gold is shown the SH3 domain, in blue the HOOK domain, in green the GK domain, and in magenta the last 12 residues C-terminal to the GK domain. The dashed lines represent the disordered parts of the molecule in both crystal forms. The residues represented in the SH3 domain constitute the proline-rich peptide binding site. In red are shown the regions in the SH3 and GK domains that participate in crystallographic contacts in both crystal forms.

Figure 5.
Figure 5. GMP Binding Site of PSD-95GMP (yellow carbon atoms) binds to the GK NMP binding domain (cyan ribbon). This interaction appears to be stabilized by an MPD molecule. The binding residues (white carbon atoms) are shown as well as two guanidine molecules.

The above figures are reprinted by permission from Cell Press: Mol Cell (2001, 8, 1313-1325) copyright 2001.

Figures were selected by the author.