1jmp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:50, 30 October 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1jmp.gif|left|200px]]
 
-
<!--
+
==Solution Structure of the Viscotoxin B==
-
The line below this paragraph, containing "STRUCTURE_1jmp", creates the "Structure Box" on the page.
+
<StructureSection load='1jmp' size='340' side='right'caption='[[1jmp]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1jmp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Viscum_album Viscum album]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JMP FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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=1jmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmp OCA], [https://pdbe.org/1jmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jmp RCSB], [https://www.ebi.ac.uk/pdbsum/1jmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jmp ProSAT]</span></td></tr>
-
{{STRUCTURE_1jmp| PDB=1jmp | SCENE= }}
+
</table>
-
 
+
== Function ==
-
'''Solution Structure of the Viscotoxin B'''
+
[https://www.uniprot.org/uniprot/THNB_VISAL THNB_VISAL] Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.[REFERENCE:3]
-
 
+
== Evolutionary Conservation ==
-
 
+
[[Image:Consurf_key_small.gif|200px|right]]
-
==Overview==
+
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/1jmp_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=1jmp ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
Viscotoxins A2 (VA2) and B (VB) are, together with viscotoxin A3 (VA3), among the most abundant viscotoxin isoforms that occur in mistletoe-derived medicines used in anti-cancer therapy. Although these isoforms have a high degree of amino-acid-sequence similarity, they are strikingly different from each other in their in vitro cytotoxic potency towards tumour cells. First, as VA3 is the only viscotoxin whose three-dimensional (3D) structure has been solved to date, we report the NMR determination of the 3D structures of VA2 and VB. Secondly, to account for the in vitro cytotoxicity discrepancy, we carried out a comparative study of the interaction of the three viscotoxins with model membranes. Although the overall 3D structure is highly conserved among the three isoforms, some discrete structural features and associated surface properties readily account for the different affinity and perturbation of model membranes. VA3 and VA2 interact in a similar way, but the weaker hydrophobic character of VA2 is thought to be mainly responsible for the apparent different affinity towards membranes. VB is much less active than the other two viscotoxins and does not insert into model membranes. This could be related to the occurrence of a single residue (Arg25) protruding outside the hydrophobic plane formed by the two amphipathic alpha-helices, through which viscotoxins are supposed to interact with plasma membranes.
Viscotoxins A2 (VA2) and B (VB) are, together with viscotoxin A3 (VA3), among the most abundant viscotoxin isoforms that occur in mistletoe-derived medicines used in anti-cancer therapy. Although these isoforms have a high degree of amino-acid-sequence similarity, they are strikingly different from each other in their in vitro cytotoxic potency towards tumour cells. First, as VA3 is the only viscotoxin whose three-dimensional (3D) structure has been solved to date, we report the NMR determination of the 3D structures of VA2 and VB. Secondly, to account for the in vitro cytotoxicity discrepancy, we carried out a comparative study of the interaction of the three viscotoxins with model membranes. Although the overall 3D structure is highly conserved among the three isoforms, some discrete structural features and associated surface properties readily account for the different affinity and perturbation of model membranes. VA3 and VA2 interact in a similar way, but the weaker hydrophobic character of VA2 is thought to be mainly responsible for the apparent different affinity towards membranes. VB is much less active than the other two viscotoxins and does not insert into model membranes. This could be related to the occurrence of a single residue (Arg25) protruding outside the hydrophobic plane formed by the two amphipathic alpha-helices, through which viscotoxins are supposed to interact with plasma membranes.
-
==About this Structure==
+
Comparative membrane interaction study of viscotoxins A3, A2 and B from mistletoe (Viscum album) and connections with their structures.,Coulon A, Mosbah A, Lopez A, Sautereau AM, Schaller G, Urech K, Rouge P, Darbon H Biochem J. 2003 Aug 15;374(Pt 1):71-8. PMID:12733989<ref>PMID:12733989</ref>
-
1JMP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Viscum_album Viscum album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMP OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Comparative membrane interaction study of viscotoxins A3, A2 and B from mistletoe (Viscum album) and connections with their structures., Coulon A, Mosbah A, Lopez A, Sautereau AM, Schaller G, Urech K, Rouge P, Darbon H, Biochem J. 2003 Aug 15;374(Pt 1):71-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12733989 12733989]
+
</div>
-
[[Category: Single protein]]
+
<div class="pdbe-citations 1jmp" style="background-color:#fffaf0;"></div>
-
[[Category: Viscum album]]
+
== References ==
-
[[Category: Bernard, C.]]
+
<references/>
-
[[Category: Coulon, A.]]
+
__TOC__
-
[[Category: Darbon, H.]]
+
</StructureSection>
-
[[Category: Mosbah, A.]]
+
[[Category: Large Structures]]
-
[[Category: Rouge, P.]]
+
-
[[Category: Urech, K.]]
+
-
[[Category: Nmr]]
+
-
[[Category: Thionin]]
+
-
[[Category: Viscotoxin]]
+
[[Category: Viscum album]]
[[Category: Viscum album]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:25:18 2008''
+
[[Category: Bernard C]]
 +
[[Category: Coulon A]]
 +
[[Category: Darbon H]]
 +
[[Category: Mosbah A]]
 +
[[Category: Rouge P]]
 +
[[Category: Urech K]]

Current revision

Solution Structure of the Viscotoxin B

PDB ID 1jmp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jmp"
Personal tools