1apf: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,329,557 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,329,557 edits
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:


==ANTHOPLEURIN-B, NMR, 20 STRUCTURES==
==ANTHOPLEURIN-B, NMR, 20 STRUCTURES==
<StructureSection load='1apf' size='340' side='right'caption='[[1apf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1apf' size='340' side='right'caption='[[1apf]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1apf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anthopleura_xanthogrammica Anthopleura xanthogrammica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1APF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1apf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anthopleura_xanthogrammica Anthopleura xanthogrammica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APF FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1apf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apf OCA], [http://pdbe.org/1apf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1apf RCSB], [http://www.ebi.ac.uk/pdbsum/1apf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1apf ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1apf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apf OCA], [https://pdbe.org/1apf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apf RCSB], [https://www.ebi.ac.uk/pdbsum/1apf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TXAB_ANTXA TXAB_ANTXA]] Binds specifically to the sodium channel (site 3) (Nav), thereby delaying its inactivation during signal transduction. Thus it strongly stimulates mammalian cardiac muscle contraction. Does not display phospholipid-binding activity. Anthopleurin-B is the most potent peptide heart stimulator isolated from the sea anemone.  
[https://www.uniprot.org/uniprot/NA1B_ANTXA NA1B_ANTXA] Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation. This toxin has the highest affinity of all anemone toxins for the mammalian sodium channel, whereas its paralog Anthopleurin-A retains the greatest capacity to discriminate between cardiac (Nav1.5/SCN5A) and neuronal sodium channels (PubMed:8916901). When tested electrophysiologically, this toxin exhibits a high affinity for multiple sodium channels with a 50-fold preference for rat cardiac (Nav1.5/SCN5A) over neuronal channels (0.1 nM versus 5 nM). When tested by ion flux, the affinities are similar and appear to have higher affinity (9 nM versus 22 nM) (PubMed:7612595, PubMed:8276803). The residue Lys-37 of this toxin has been shown to interact with channel Nav1.5 (residue Asp-1612 in rat and Asp-1610 in human), which is located in the DIV S3-S4 linker (corresponding to channel site 3) (PubMed:24898004, PubMed:9417050). Selectively modifies sodium channel inactivation from the open state with little effect on channel activation or on inactivation from closed states (By similarity). Does not display phospholipid-binding activities, suggesting that the domain IV S3-S4 linker is located at the extracellular surface and not buried in the phospholipid bilayer (PubMed:15632158).[UniProtKB:P01530]<ref>PMID:15632158</ref> <ref>PMID:24898004</ref> <ref>PMID:7612595</ref> <ref>PMID:8276803</ref> <ref>PMID:8916901</ref> <ref>PMID:9306007</ref> <ref>PMID:9417050</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 13: Line 14:
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1apf_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1apf_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
Line 33: Line 34:
[[Category: Anthopleura xanthogrammica]]
[[Category: Anthopleura xanthogrammica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Monks, S A]]
[[Category: Monks SA]]
[[Category: Norton, R S]]
[[Category: Norton RS]]
[[Category: Pallaghy, P K]]
[[Category: Pallaghy PK]]
[[Category: Scanlon, M J]]
[[Category: Scanlon MJ]]
[[Category: Cardiac stimulant]]
[[Category: Sea anemone]]
[[Category: Toxin]]
Retrieved from "https://proteopedia.org/1apf"