3dih: Difference between revisions

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New page: '''Unreleased structure''' The entry 3dih is ON HOLD Authors: Turk, D., Guncar, G., Krizaj, I. Description: Crystal structure of ammodytin L ''Page seeded by [http://oca.weizmann.ac.i...
 
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'''Unreleased structure'''


The entry 3dih is ON HOLD
==Crystal structure of ammodytin L==
<StructureSection load='3dih' size='340' side='right'caption='[[3dih]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3dih]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vipera_ammodytes_ammodytes Vipera ammodytes ammodytes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DIH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=3dih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dih OCA], [https://pdbe.org/3dih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dih RCSB], [https://www.ebi.ac.uk/pdbsum/3dih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dih ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PA2HL_VIPAA PA2HL_VIPAA] Snake venom phospholipase A2 homolog that is very active in inducing myonecrosis in vivo and shows a potent calcium-independent membrane-damaging activity in vitro, most probably by binding and incorporating in the membrane. Also acts as a presynaptic neurotoxin.<ref>PMID:10653156</ref> <ref>PMID:11005629</ref> <ref>PMID:1765075</ref> <ref>PMID:17927217</ref> <ref>PMID:7662700</ref> <ref>PMID:8835336</ref> <ref>PMID:8973554</ref> <ref>PMID:9514950</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/3dih_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dih ConSurf].
<div style="clear:both"></div>


Authors: Turk, D., Guncar, G., Krizaj, I.
==See Also==
 
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
Description: Crystal structure of ammodytin L
*[[Phospholipase A2 homolog|Phospholipase A2 homolog]]
 
== References ==
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 13:07:49 2008''
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vipera ammodytes ammodytes]]
[[Category: Guncar G]]
[[Category: Krizaj I]]
[[Category: Turk D]]

Latest revision as of 08:45, 17 October 2024

Crystal structure of ammodytin LCrystal structure of ammodytin L

Structural highlights

3dih is a 1 chain structure with sequence from Vipera ammodytes ammodytes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PA2HL_VIPAA Snake venom phospholipase A2 homolog that is very active in inducing myonecrosis in vivo and shows a potent calcium-independent membrane-damaging activity in vitro, most probably by binding and incorporating in the membrane. Also acts as a presynaptic neurotoxin.[1] [2] [3] [4] [5] [6] [7] [8]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Horvat-Znidarsic I, Suput D, Gubensek F. The effect of ammodytin L on frog neuromuscular junction. Pflugers Arch. 2000;439(3 Suppl):R102-3. PMID:10653156
  2. ↑ Frangez R, Krizaj I, Gubensek F, Suput D. Effects of ammodytin L on miniature and endplate potentials in neuromuscular junction of frog m. cutaneus pectoris. Pflugers Arch. 2000;440(5 Suppl):R101-2. PMID:11005629
  3. ↑ Krizaj I, Bieber AL, Ritonja A, Gubensek F. The primary structure of ammodytin L, a myotoxic phospholipase A2 homologue from Vipera ammodytes venom. Eur J Biochem. 1991 Dec 18;202(3):1165-8. PMID:1765075
  4. ↑ Petan T, Krizaj I, Pungercar J. Restoration of enzymatic activity in a Ser-49 phospholipase A2 homologue decreases its Ca(2+)-independent membrane-damaging activity and increases its toxicity. Biochemistry. 2007 Nov 6;46(44):12795-809. Epub 2007 Oct 10. PMID:17927217 doi:http://dx.doi.org/10.1021/bi701304e
  5. ↑ Incerpi S, de Vito P, Luly P, Rufini S. Effect of ammodytin L from Vipera ammodytes on L-6 cells from rat skeletal muscle. Biochim Biophys Acta. 1995 Aug 31;1268(2):137-42. PMID:7662700
  6. ↑ Bernardini S, Cannata S, Filoni S, Luly P, Rufini S. Effect of ammodytin L from the venom of Vipera ammodytes on Xenopus laevis differentiated muscle fibres and regenerating limbs. Toxicon. 1996 Jan;34(1):81-90. PMID:8835336
  7. ↑ Rufini S, Cesaroni MP, Balestro N, Luly P. Proliferative effect of ammodytin L from the venom of Vipera ammodytes on 208F rat fibroblasts in culture. Biochem J. 1996 Dec 1;320 ( Pt 2):467-72. PMID:8973554
  8. ↑ Pungercar J, Vucemilo N, Faure G, Bon C, Verheij HM, Gubensek F, Krizaj I. Ammodytin L, an inactive phospholipase A2 homologue with myotoxicity in mice, binds to the presynaptic acceptor of the beta-neurotoxic ammodytoxin C in Torpedo: an indication for a phospholipase A2 activity-independent mechanism of action of beta-neurotoxins in fish? Biochem Biophys Res Commun. 1998 Mar 17;244(2):514-8. PMID:9514950

3dih, resolution 2.60Å

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