1zbd: Difference between revisions

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[[Image:1zbd.~~gif~~|left|200px]]

[[Image:1zbd.png|left|200px]]

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

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

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_10025402}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10025402 is the PubMed ID number.

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==About this Structure==

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[[Category: Rabphilin]]

[[Category: Synaptic exocytosis]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 17~~:25:01 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:15:54 2008''

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-[[Image:1zbd.gif|left|200px]]
+{{Seed}}
+[[Image:1zbd.png|left|200px]]
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 {{STRUCTURE_1zbd|  PDB=1zbd  |  SCENE=  }}
-'''STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10025402}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10025402 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10025402}}
 ==About this Structure==
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 [[Category: Rabphilin]]
 [[Category: Synaptic exocytosis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:25:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:15:54 2008''