2dfk

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'''Crystal structure of the CDC42-Collybistin II complex'''<br />
'''Crystal structure of the CDC42-Collybistin II complex'''<br />
==Overview==
==Overview==
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The synaptic localization of ion channel receptors is essential for, efficient synaptic transmission and the precise regulation of diverse, neuronal functions. In the central nervous system, ion channel receptors, reside in the postsynaptic membrane where they are juxtaposed to, presynaptic terminals. For proper function, these ion channels have to be, anchored to the cytoskeleton, and in the case of the inhibitory glycine, and gamma-amino-butyric acid type A (GABA(A)) receptors this interaction, is mediated by a gephyrin centered scaffold. Highlighting its central role, in this receptor anchoring scaffold, gephyrin interacts with a number of, proteins, including the neurospecific guanine nucleotide exchange factor, collybistin. Collybistin belongs to the Dbl family of guanine nucleotide, exchange factors, occurs in multiple splice variants, and is specific for, Cdc42, a small GTPase belonging to the Rho family. The 2.3 Angstroms, resolution crystal structure of the Cdc42-collybistin II complex reveals a, novel conformation of the switch I region of Cdc42. It also provides the, first direct observation of structural changes in the relative orientation, of the Dbl-homology domain and the pleckstrin-homology domain in the same, Dbl family protein. Biochemical data indicate that gephyrin negatively, regulates collybistin activity.
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The synaptic localization of ion channel receptors is essential for efficient synaptic transmission and the precise regulation of diverse neuronal functions. In the central nervous system, ion channel receptors reside in the postsynaptic membrane where they are juxtaposed to presynaptic terminals. For proper function, these ion channels have to be anchored to the cytoskeleton, and in the case of the inhibitory glycine and gamma-amino-butyric acid type A (GABA(A)) receptors this interaction is mediated by a gephyrin centered scaffold. Highlighting its central role in this receptor anchoring scaffold, gephyrin interacts with a number of proteins, including the neurospecific guanine nucleotide exchange factor collybistin. Collybistin belongs to the Dbl family of guanine nucleotide exchange factors, occurs in multiple splice variants, and is specific for Cdc42, a small GTPase belonging to the Rho family. The 2.3 Angstroms resolution crystal structure of the Cdc42-collybistin II complex reveals a novel conformation of the switch I region of Cdc42. It also provides the first direct observation of structural changes in the relative orientation of the Dbl-homology domain and the pleckstrin-homology domain in the same Dbl family protein. Biochemical data indicate that gephyrin negatively regulates collybistin activity.
==About this Structure==
==About this Structure==
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2DFK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DFK OCA].
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2DFK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DFK OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Connelly, J.J.]]
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[[Category: Connelly, J J.]]
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[[Category: Kim, E.Y.]]
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[[Category: Kim, E Y.]]
[[Category: Kirsch, J.]]
[[Category: Kirsch, J.]]
[[Category: Nassar, N.]]
[[Category: Nassar, N.]]
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[[Category: ph domain]]
[[Category: ph domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:31:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:17 2008''

Revision as of 14:58, 21 February 2008


2dfk, resolution 2.15Å

Drag the structure with the mouse to rotate

Crystal structure of the CDC42-Collybistin II complex

Overview

The synaptic localization of ion channel receptors is essential for efficient synaptic transmission and the precise regulation of diverse neuronal functions. In the central nervous system, ion channel receptors reside in the postsynaptic membrane where they are juxtaposed to presynaptic terminals. For proper function, these ion channels have to be anchored to the cytoskeleton, and in the case of the inhibitory glycine and gamma-amino-butyric acid type A (GABA(A)) receptors this interaction is mediated by a gephyrin centered scaffold. Highlighting its central role in this receptor anchoring scaffold, gephyrin interacts with a number of proteins, including the neurospecific guanine nucleotide exchange factor collybistin. Collybistin belongs to the Dbl family of guanine nucleotide exchange factors, occurs in multiple splice variants, and is specific for Cdc42, a small GTPase belonging to the Rho family. The 2.3 Angstroms resolution crystal structure of the Cdc42-collybistin II complex reveals a novel conformation of the switch I region of Cdc42. It also provides the first direct observation of structural changes in the relative orientation of the Dbl-homology domain and the pleckstrin-homology domain in the same Dbl family protein. Biochemical data indicate that gephyrin negatively regulates collybistin activity.

About this Structure

2DFK is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of Cdc42 in complex with collybistin II, a gephyrin-interacting guanine nucleotide exchange factor., Xiang S, Kim EY, Connelly JJ, Nassar N, Kirsch J, Winking J, Schwarz G, Schindelin H, J Mol Biol. 2006 May 26;359(1):35-46. Epub 2006 Mar 29. PMID:16616186

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