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PDBsum entry 1jxo
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Structural protein
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PDB id
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1jxo
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural characterization of the intramolecular interaction between the sh3 and guanylate kinase domains of psd-95.
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Authors
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G.A.Tavares,
E.H.Panepucci,
A.T.Brunger.
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Ref.
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Mol Cell, 2001,
8,
1313-1325.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2001,
8,
1313-1325)
copyright 2001.
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