1q3p

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(New page: 200px<br /><applet load="1q3p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q3p, resolution 2.25&Aring;" /> '''Crystal structure of...)
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[[Image:1q3p.jpg|left|200px]]<br /><applet load="1q3p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1q3p, resolution 2.25&Aring;" />
caption="1q3p, resolution 2.25&Aring;" />
'''Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization'''<br />
'''Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization'''<br />
==Overview==
==Overview==
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The Shank/proline-rich synapse-associated protein family of multidomain, proteins is known to play an important role in the organization of, synaptic multiprotein complexes. For instance, the Shank PDZ domain binds, to the C termini of guanylate kinase-associated proteins, which in turn, interact with the guanylate kinase domain of postsynaptic density-95, scaffolding proteins. Here we describe the crystal structures of Shank1, PDZ in its peptide free form and in complex with the C-terminal, hexapeptide (EAQTRL) of guanylate kinase-associated protein (GKAP1a), determined at 1.8- and 2.25-A resolutions, respectively. The structure, shows the typical class I PDZ interaction of PDZ-peptide complex with the, consensus sequence -X-(Thr/Ser)-X-Leu. In addition, Asp-634 within the, Shank1 PDZ domain recognizes the positively charged Arg at -1 position and, hydrogen bonds, and salt bridges between Arg-607 and the side chains of, the ligand at -3 and -5 positions contribute further to the recognition of, the peptide ligand. Remarkably, whether free or complexed, Shank1 PDZ, domains form dimers with a conserved beta B/beta C loop and N-terminal, beta A strands, suggesting a novel model of PDZ-PDZ homodimerization. This, implies that antiparallel dimerization through the N-terminal beta A, strands could be a common configuration among PDZ dimers. Within the, dimeric structure, the two-peptide binding sites are arranged so that the, N termini of the bound peptide ligands are in close proximity and oriented, toward the 2-fold axis of the dimer. This configuration may provide a, means of facilitating dimeric organization of PDZ-target assemblies.
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The Shank/proline-rich synapse-associated protein family of multidomain proteins is known to play an important role in the organization of synaptic multiprotein complexes. For instance, the Shank PDZ domain binds to the C termini of guanylate kinase-associated proteins, which in turn interact with the guanylate kinase domain of postsynaptic density-95 scaffolding proteins. Here we describe the crystal structures of Shank1 PDZ in its peptide free form and in complex with the C-terminal hexapeptide (EAQTRL) of guanylate kinase-associated protein (GKAP1a) determined at 1.8- and 2.25-A resolutions, respectively. The structure shows the typical class I PDZ interaction of PDZ-peptide complex with the consensus sequence -X-(Thr/Ser)-X-Leu. In addition, Asp-634 within the Shank1 PDZ domain recognizes the positively charged Arg at -1 position and hydrogen bonds, and salt bridges between Arg-607 and the side chains of the ligand at -3 and -5 positions contribute further to the recognition of the peptide ligand. Remarkably, whether free or complexed, Shank1 PDZ domains form dimers with a conserved beta B/beta C loop and N-terminal beta A strands, suggesting a novel model of PDZ-PDZ homodimerization. This implies that antiparallel dimerization through the N-terminal beta A strands could be a common configuration among PDZ dimers. Within the dimeric structure, the two-peptide binding sites are arranged so that the N termini of the bound peptide ligands are in close proximity and oriented toward the 2-fold axis of the dimer. This configuration may provide a means of facilitating dimeric organization of PDZ-target assemblies.
==About this Structure==
==About this Structure==
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1Q3P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q3P OCA].
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1Q3P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q3P OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Eom, S.H.]]
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[[Category: Eom, S H.]]
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[[Category: Im, Y.J.]]
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[[Category: Im, Y J.]]
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[[Category: Kang, G.B.]]
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[[Category: Kang, G B.]]
[[Category: Kim, E.]]
[[Category: Kim, E.]]
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[[Category: Lee, J.H.]]
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[[Category: Lee, J H.]]
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[[Category: Park, S.H.]]
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[[Category: Park, S H.]]
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[[Category: Park, S.J.]]
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[[Category: Park, S J.]]
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[[Category: Rho, S.H.]]
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[[Category: Rho, S H.]]
[[Category: crystal structure]]
[[Category: crystal structure]]
[[Category: gkap]]
[[Category: gkap]]
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[[Category: shank]]
[[Category: shank]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:21:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:33 2008''

Revision as of 12:35, 21 February 2008


1q3p, resolution 2.25Å

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Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization

Overview

The Shank/proline-rich synapse-associated protein family of multidomain proteins is known to play an important role in the organization of synaptic multiprotein complexes. For instance, the Shank PDZ domain binds to the C termini of guanylate kinase-associated proteins, which in turn interact with the guanylate kinase domain of postsynaptic density-95 scaffolding proteins. Here we describe the crystal structures of Shank1 PDZ in its peptide free form and in complex with the C-terminal hexapeptide (EAQTRL) of guanylate kinase-associated protein (GKAP1a) determined at 1.8- and 2.25-A resolutions, respectively. The structure shows the typical class I PDZ interaction of PDZ-peptide complex with the consensus sequence -X-(Thr/Ser)-X-Leu. In addition, Asp-634 within the Shank1 PDZ domain recognizes the positively charged Arg at -1 position and hydrogen bonds, and salt bridges between Arg-607 and the side chains of the ligand at -3 and -5 positions contribute further to the recognition of the peptide ligand. Remarkably, whether free or complexed, Shank1 PDZ domains form dimers with a conserved beta B/beta C loop and N-terminal beta A strands, suggesting a novel model of PDZ-PDZ homodimerization. This implies that antiparallel dimerization through the N-terminal beta A strands could be a common configuration among PDZ dimers. Within the dimeric structure, the two-peptide binding sites are arranged so that the N termini of the bound peptide ligands are in close proximity and oriented toward the 2-fold axis of the dimer. This configuration may provide a means of facilitating dimeric organization of PDZ-target assemblies.

About this Structure

1Q3P is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization., Im YJ, Lee JH, Park SH, Park SJ, Rho SH, Kang GB, Kim E, Eom SH, J Biol Chem. 2003 Nov 28;278(48):48099-104. Epub 2003 Sep 3. PMID:12954649

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