1auv: Difference between revisions

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

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

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~~'''~~STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN~~'''~~

===STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN===

~~==Overview==~~

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~~Synapsins are abundant synaptic vesicle proteins with an essential regulatory function in the nerve terminal. We determined the crystal structure of a fragment (synC) consisting of residues 110~~-~~420 of bovine synapsin I; synC coincides with the large middle domain (C~~-~~domain)~~, the ~~most conserved domain of synapsins. SynC molecules are folded into compact domains and form closely associated dimers. SynC monomers are strikingly similar in structure~~ to ~~a family of ATP-utilizing enzymes, which includes glutathione synthetase and D-alanine~~:~~D-alanine ligase~~. ~~SynC binds ATP in a Ca2+-dependent manner~~. ~~The crystal structure of synC in complex with ATPgammaS and Ca2+ explains~~ the ~~preference of synC for Ca2+ over Mg2+~~. ~~Our results suggest that synapsins may also be ATP~~-~~utilizing enzymes.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9463376}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9463376 is the PubMed ID number.

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==About this Structure==

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[[Category: Synapse]]

[[Category: Synapsin ia c-domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 10~~:43:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:38:27 2008''

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-[[Image:1auv.gif|left|200px]]
+{{Seed}}
+[[Image:1auv.png|left|200px]]
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 {{STRUCTURE_1auv|  PDB=1auv  |  SCENE=  }}
-'''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN'''
+===STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN===
-==Overview==
+<!--
-Synapsins are abundant synaptic vesicle proteins with an essential regulatory function in the nerve terminal. We determined the crystal structure of a fragment (synC) consisting of residues 110-420 of bovine synapsin I; synC coincides with the large middle domain (C-domain), the most conserved domain of synapsins. SynC molecules are folded into compact domains and form closely associated dimers. SynC monomers are strikingly similar in structure to a family of ATP-utilizing enzymes, which includes glutathione synthetase and D-alanine:D-alanine ligase. SynC binds ATP in a Ca2+-dependent manner. The crystal structure of synC in complex with ATPgammaS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.
+The line below this paragraph, {{ABSTRACT_PUBMED_9463376}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9463376 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9463376}}
 ==About this Structure==
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 [[Category: Synapse]]
 [[Category: Synapsin ia c-domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:43:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:38:27 2008''