1q01: Difference between revisions

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[[Image:1q01.gif|left|200px]]<br /><applet load="1q01" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1q01" />
'''Lebetin peptides, a new class of potent aggregation inhibitors'''<br />


==About this Structure==
==Lebetin peptides, a new class of potent aggregation inhibitors==
1Q01 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Macrovipera_lebetina Macrovipera lebetina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q01 OCA].  
<StructureSection load='1q01' size='340' side='right'caption='[[1q01]]' scene=''>
[[Category: Macrovipera lebetina]]
== Structural highlights ==
[[Category: Single protein]]
<table><tr><td colspan='2'>[[1q01]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Macrovipera_lebetinus Macrovipera lebetinus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q01 FirstGlance]. <br>
[[Category: Ayeb, M El.]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 24 models</td></tr>
[[Category: Darbon, H.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q01 OCA], [https://pdbe.org/1q01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q01 RCSB], [https://www.ebi.ac.uk/pdbsum/1q01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q01 ProSAT]</span></td></tr>
[[Category: Ganzalez, M J.]]
</table>
[[Category: Giralt, E.]]
== Function ==
[[Category: Mabrouk, K.]]
[https://www.uniprot.org/uniprot/LEB_MACLB LEB_MACLB] Lebetins inhibit platelet aggregation induced by thrombin, collagen and PAF-acether. Human platelet aggregation induced by thrombin is inhibited by synthetic lebetin-1-alpha, lebetin-1-beta, lebetin-1-gamma, lebetin-2-alpha and lebetin-2-beta with IC(50) values of 140, 32, 5, 2.5 and 2.8 nM, respectively. Lebetins also inhibit fibrinogen-induced aggregation of alpha-chymotrypsin-treated platelets as well as in vivo collagen-induced thrombocytopenia in rats. Lebetins are not toxic upon intravenous injection into mice and rats.<ref>PMID:11910186</ref> <ref>PMID:8769304</ref> <ref>PMID:9839678</ref>
[[Category: Marrakchi, N.]]
== References ==
[[Category: Mosbah, A.]]
<references/>
[[Category: Rietschoten, J Van.]]
__TOC__
[[Category: Rochat, H.]]
</StructureSection>
[[Category: Sabatier, J M.]]
[[Category: Large Structures]]
[[Category: beta-bulged hairpain]]
[[Category: Macrovipera lebetinus]]
 
[[Category: Darbon H]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:22 2008''
[[Category: El Ayeb M]]
[[Category: Ganzalez MJ]]
[[Category: Giralt E]]
[[Category: Mabrouk K]]
[[Category: Marrakchi N]]
[[Category: Mosbah A]]
[[Category: Rochat H]]
[[Category: Sabatier JM]]
[[Category: Van Rietschoten J]]

Latest revision as of 10:14, 30 October 2024

Lebetin peptides, a new class of potent aggregation inhibitorsLebetin peptides, a new class of potent aggregation inhibitors

Structural highlights

1q01 is a 1 chain structure with sequence from Macrovipera lebetinus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 24 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEB_MACLB Lebetins inhibit platelet aggregation induced by thrombin, collagen and PAF-acether. Human platelet aggregation induced by thrombin is inhibited by synthetic lebetin-1-alpha, lebetin-1-beta, lebetin-1-gamma, lebetin-2-alpha and lebetin-2-beta with IC(50) values of 140, 32, 5, 2.5 and 2.8 nM, respectively. Lebetins also inhibit fibrinogen-induced aggregation of alpha-chymotrypsin-treated platelets as well as in vivo collagen-induced thrombocytopenia in rats. Lebetins are not toxic upon intravenous injection into mice and rats.[1] [2] [3]

References

  1. ↑ Marrakchi N, Mabrouk K, Regaya I, Sarray S, Fathallah M, Rochat H, El Ayeb M. Lebetin peptides: potent platelet aggregation inhibitors. Haemostasis. 2001 May-Dec;31(3-6):207-10. PMID:11910186 doi:http://dx.doi.org/48064
  2. ↑ Barbouche R, Marrakchi N, Mansuelle P, Krifi M, Fenouillet E, Rochat H, el Ayeb M. Novel anti-platelet aggregation polypeptides from Vipera lebetina venom: isolation and characterization. FEBS Lett. 1996 Aug 19;392(1):6-10. PMID:8769304
  3. ↑ Barbouche R, Marrakchi N, Mabrouk K, Krifi MN, Van Rietschoten J, Fenouillet E, El Ayeb M, Rochat H. Anti-platelet activity of the peptides composing the lebetin 1 family, a new class of inhibitors of platelet aggregation. Toxicon. 1998 Dec;36(12):1939-47. PMID:9839678
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