1zbd

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(New page: 200px<br /><applet load="1zbd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zbd, resolution 2.6&Aring;" /> '''STRUCTURAL BASIS OF R...)
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[[Image:1zbd.gif|left|200px]]<br /><applet load="1zbd" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zbd.gif|left|200px]]<br /><applet load="1zbd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zbd, resolution 2.6&Aring;" />
caption="1zbd, resolution 2.6&Aring;" />
'''STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A'''<br />
'''STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A'''<br />
==Overview==
==Overview==
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The small G protein Rab3A plays an important role in the regulation of, neurotransmitter release. The crystal structure of activated, Rab3A/GTP/Mg2+ bound to the effector domain of rabphilin-3A was solved to, 2.6 A resolution. Rabphilin-3A contacts Rab3A in two distinct areas. The, first interface involves the Rab3A switch I and switch II regions, which, are sensitive to the nucleotide-binding state of Rab3A. The second, interface consists of a deep pocket in Rab3A that interacts with a SGAWFF, structural element of rabphilin-3A. Sequence and structure analysis, and, biochemical data suggest that this pocket, or Rab, complementarity-determining region (RabCDR), establishes a specific, interaction between each Rab protein and its effectors. RabCDRs could be, major determinants of effector specificity during vesicle trafficking and, fusion.
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The small G protein Rab3A plays an important role in the regulation of neurotransmitter release. The crystal structure of activated Rab3A/GTP/Mg2+ bound to the effector domain of rabphilin-3A was solved to 2.6 A resolution. Rabphilin-3A contacts Rab3A in two distinct areas. The first interface involves the Rab3A switch I and switch II regions, which are sensitive to the nucleotide-binding state of Rab3A. The second interface consists of a deep pocket in Rab3A that interacts with a SGAWFF structural element of rabphilin-3A. Sequence and structure analysis, and biochemical data suggest that this pocket, or Rab complementarity-determining region (RabCDR), establishes a specific interaction between each Rab protein and its effectors. RabCDRs could be major determinants of effector specificity during vesicle trafficking and fusion.
==About this Structure==
==About this Structure==
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1ZBD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN, MG and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZBD OCA].
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1ZBD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZBD OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Brunger, A.T.]]
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[[Category: Brunger, A T.]]
[[Category: Ostermeier, C.]]
[[Category: Ostermeier, C.]]
[[Category: GTP]]
[[Category: GTP]]
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[[Category: synaptic exocytosis]]
[[Category: synaptic exocytosis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:21:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:52 2008''

Revision as of 14:13, 21 February 2008

Image:1zbd.gif

1zbd, resolution 2.6Å

Drag the structure with the mouse to rotate

STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A

Overview

The small G protein Rab3A plays an important role in the regulation of neurotransmitter release. The crystal structure of activated Rab3A/GTP/Mg2+ bound to the effector domain of rabphilin-3A was solved to 2.6 A resolution. Rabphilin-3A contacts Rab3A in two distinct areas. The first interface involves the Rab3A switch I and switch II regions, which are sensitive to the nucleotide-binding state of Rab3A. The second interface consists of a deep pocket in Rab3A that interacts with a SGAWFF structural element of rabphilin-3A. Sequence and structure analysis, and biochemical data suggest that this pocket, or Rab complementarity-determining region (RabCDR), establishes a specific interaction between each Rab protein and its effectors. RabCDRs could be major determinants of effector specificity during vesicle trafficking and fusion.

About this Structure

1ZBD is a Protein complex structure of sequences from Rattus norvegicus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A., Ostermeier C, Brunger AT, Cell. 1999 Feb 5;96(3):363-74. PMID:10025402

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