This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1fvl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:17, 27 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1fvl.gif|left|200px]]<br /><applet load="1fvl" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1fvl" />
 
-
'''THE NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF FLAVORIDIN, AN ANTAGONIST OF THE PLATELET GP IIB-IIIA RECEPTOR'''<br />
 
-
==Overview==
+
==THE NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF FLAVORIDIN, AN ANTAGONIST OF THE PLATELET GP IIB-IIIA RECEPTOR==
-
The snake venom protein flavoridin, a polypeptide of 70 amino acid residues, is a potent inhibitor of blood platelet aggregation. It binds to cell-surface integrin receptors such as the fibrinogen receptor glycoprotein IIb/IIIa. The inhibitory properties of flavoridin have been attributed to the tripeptide segment Arg-Gly-Asp (residues 49 to 51). This paper describes the determination of the three-dimensional structure of flavoridin in aqueous solution based on two-dimensional nuclear magnetic resonance spectroscopy. A family of 18 conformers was selected to characterize the solution structure. The molecule comprises two structural domains, an N-terminal unit extending from residues 1 to 25, and a C-terminal unit from residues 26 to 70. Whereas the mutual spatial orientation of these regions is not well defined, each one is well organized within itself. The segment 26 to 70, which is homologous to the sequence of the snake toxins echistatin and eristostatin, shows an average value of 1.0 A for the root-mean-square deviations of the backbone atoms among the 18 conformers. The structure of flavoridin consists essentially of non-repetitive elements such as tight turns and loops, whose location and conformation are characterized in this paper. With the exception of two short regions of antiparallel beta-sheet, no classic element of protein secondary structure is present. The six disulphide bridges, which have been mapped by applying a novel computational strategy (see accompanying paper), are the dominant organizational feature of the polypeptide fold of flavoridin. Two of the bridges are located in the N-terminal domain, three in the C-terminal domain and one connects the two structural units. The mobile RGD recognition sequence for integrins is located peripheral to the core region of the C-terminal domain at the most exposed end of a nine residue loop structure, which is attached to a short beta-sheet. The C terminus is close to this loop structure.
+
<StructureSection load='1fvl' size='340' side='right'caption='[[1fvl]]' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1fvl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Protobothrops_flavoviridis Protobothrops flavoviridis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FVL FirstGlance]. <br>
-
1FVL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trimeresurus_flavoviridis Trimeresurus flavoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVL OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1fvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvl OCA], [https://pdbe.org/1fvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fvl RCSB], [https://www.ebi.ac.uk/pdbsum/1fvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fvl ProSAT]</span></td></tr>
-
==Reference==
+
</table>
-
The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIb-IIIa receptor., Senn H, Klaus W, J Mol Biol. 1993 Aug 5;232(3):907-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8355277 8355277]
+
== Function ==
-
[[Category: Single protein]]
+
[https://www.uniprot.org/uniprot/VM2FL_PROFL VM2FL_PROFL] Snake venom metalloproteinase: impairs hemostasis in the envenomed animal. Disintegrin flavoridin: inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3) (By similarity).
-
[[Category: Trimeresurus flavoviridis]]
+
== Evolutionary Conservation ==
-
[[Category: Klaus, W.]]
+
[[Image:Consurf_key_small.gif|200px|right]]
-
[[Category: Senn, H.]]
+
Check<jmol>
-
[[Category: gp iib/iiia antagonist]]
+
<jmolCheckbox>
-
 
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/1fvl_consurf.spt"</scriptWhenChecked>
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:07 2008''
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1fvl ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Protobothrops flavoviridis]]
 +
[[Category: Klaus W]]
 +
[[Category: Senn H]]

Current revision

THE NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF FLAVORIDIN, AN ANTAGONIST OF THE PLATELET GP IIB-IIIA RECEPTOR

PDB ID 1fvl

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/1fvl"
Personal tools