Proteopedia - User contributions [en]

Talk:Neuroligin

2015-06-03T13:11:50Z

Pascale Marchot: New page: Hi all, the "Crystal Structure of human Neuroligin 3be8" figure is useless since it shows four molecules (crystal unit cell?) while the functional form of neuroligins is the four-helix bun...

Hi all, the "Crystal Structure of human Neuroligin 3be8" figure is useless since it shows four molecules (crystal unit cell?) while the functional form of neuroligins is the four-helix bundle dimer. Regards - Pascale

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Neuroligin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Neuroligin

2015-06-03T13:06:53Z

Pascale Marchot:

[[Image:3be8a.png|left|200px|thumb|Crystal Structure of human Neuroligin [[3be8]]]]
{{STRUCTURE_3b3q| PDB=3b3q | SIZE=400| SCENE= |right|CAPTION=Dimer of two mouse neuroligin-1 cholinesterase-like domains (grey and green) in complex with two neurexin-beta1 LNS6 domains (pink and cyan) and Ca+2 ions (green) [[3b3q]] }}

[[Neuroligin|Neuroligins]] (NLGN) are a family of postsynaptic proteins which bind to the presynaptic [[Neurexins]] (NRXN) to form a complex which attaches neurons. In humans the NLGN family contains 4 to 5 members that are numbered 1, 2, 3, 4X and 5 or 4Y. See [[Neurodevelopmental Disorders]].

For Structural Analysis of Neuroligin, See: [[Neuroligin-Neurexin Interaction]]

{{TOC limit|limit=2}}

== 3D Structures of Neuroligin ==

{{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

* Neuroligin

**[[3bl8]] - mNLGN-2 cholinesterase domain – mouse 
**[[3be8]] - hNLGN-4 cholinesterase domain – human 
**[[3bix]] - rNLGN-1 cholinesterase domain - rat 

* Neuroligin+neurexin

**[[2xb6]], [[2wqz]] – hNLGN-4 cholinesterase domain+NRXN-1β LNS domain 
**[[3b3q]] - mNLGN-4 cholinesterase domain+NRXN-1β LNS domain 
**[[3biw]] - rNLGN-1 cholinesterase domain+NRXN-1β LNS domain 
**[[3vkf]] - rNLGN-1 cholinesterase domain + bNRXN-1β LNS domain
}}
[[Category:Topic Page]]

Neuroligin

2015-06-03T13:06:17Z

Pascale Marchot:

[[Image:3be8a.png|left|200px|thumb|Crystal Structure of human Neuroligin [[3be8]]]]
{{STRUCTURE_3b3q| PDB=3b3q | SIZE=400| SCENE= |right|CAPTION=Dimer of two mouse neuroligin-1 cholinesterase-like domains (grey and green) in complex with two neurexin-beta1 LNS6 domain (pink and cyan) and Ca+2 ions (green) [[3b3q]] }}

[[Neuroligin|Neuroligins]] (NLGN) are a family of postsynaptic proteins which bind to the presynaptic [[Neurexins]] (NRXN) to form a complex which attaches neurons. In humans the NLGN family contains 4 to 5 members that are numbered 1, 2, 3, 4X and 5 or 4Y. See [[Neurodevelopmental Disorders]].

For Structural Analysis of Neuroligin, See: [[Neuroligin-Neurexin Interaction]]

{{TOC limit|limit=2}}

== 3D Structures of Neuroligin ==

{{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|

* Neuroligin

**[[3bl8]] - mNLGN-2 cholinesterase domain – mouse 
**[[3be8]] - hNLGN-4 cholinesterase domain – human 
**[[3bix]] - rNLGN-1 cholinesterase domain - rat 

* Neuroligin+neurexin

**[[2xb6]], [[2wqz]] – hNLGN-4 cholinesterase domain+NRXN-1β LNS domain 
**[[3b3q]] - mNLGN-4 cholinesterase domain+NRXN-1β LNS domain 
**[[3biw]] - rNLGN-1 cholinesterase domain+NRXN-1β LNS domain 
**[[3vkf]] - rNLGN-1 cholinesterase domain + bNRXN-1β LNS domain
}}
[[Category:Topic Page]]

Talk:Fasciculin

2012-08-01T17:42:24Z

Pascale Marchot:

Dear Proteopedia fellows and fasciculin users,

Please note that fasciculin variants require Arabic numerals (i.e., fasciculin 1, 2, 3 or Fas1, Fas2, Fas3), not Roman numerals (FasI, FasII, FasIII).

Reason #1 is that this is the way they were named and numbered by their finders, so why should we change this?

Reason #2 is that the choice of Arabic versus Roman numerals when naming a peptidic toxin is not only based on the godfather's choice but also relates to a code shared by toxinologists during the previous century. Indeed, in these old times the first step of toxin purification from a whole venom involved gel filtration, leading to rough fractions numbered with Roman numerals, then ion exchange chromatography, leading to fractions numbered with Arabic numerals. For those cases where a third step was required, lower-case letters could be added after the Arabic numerals.

This code might sound out of date now that more sophisticated means like HPLC etc are used for toxin purification. Yet, simply from their names, a toxinologist knows that fasciculins Fas1 and Fas2, which were purified from the same venom 3 decades ago, were separated from each other by ion exchange chromatography...

Talk:Fasciculin

2012-08-01T17:24:49Z

Pascale Marchot: New page: Dear Proteopedikers, Fasciculin variants require Arabic numerals (i.e., fasciculin 1, 2, 3 or Fas1, Fas2, Fas3), not Roman numerals (FasI, FasII, FasIII). Reason #1 is that this is the w...

Dear Proteopedikers,

Fasciculin variants require Arabic numerals (i.e., fasciculin 1, 2, 3 or Fas1, Fas2, Fas3), not Roman numerals (FasI, FasII, FasIII).

Reason #1 is that this is the way they were named by their finders and are not supposed to be renamed at random.

Reason #2 is that the choice of Arabic versus Roman numerals when naming a peptidic toxin is not only based on the godfather's choice but, instead, relates to a code shared by toxinologists during the previous century. Indeed, in these "ancient times" the first step of toxin purification from a whole venom involved gel-filtration, leading to rough fractions numbered with Roman numerals, then re-chromatography of these fractions by ion exchange, leading to fractions numbered with Arabic numerals. For those cases where a third step was required, lower-case letters were added after the Arabic numeral.

I admit that this code might sound out of date now that more sophisticated means such as HPLC etc are used for toxin purification. Yet, simply from their names, an "ancient" toxinologist knows that fasciculins Fas1 and Fas2 were separated from each other by ion exchange chromatography...