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1fvl

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Revision as of 07:36, 19 June 2019

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

Structural highlights

1fvl is a 1 chain structure with sequence from Trimeresurus flavoviridis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

Evolutionary Conservation

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

Publication Abstract from PubMed

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.

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:8355277^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Senn H, Klaus W. The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIb-IIIa receptor. J Mol Biol. 1993 Aug 5;232(3):907-25. PMID:8355277 doi:http://dx.doi.org/10.1006/jmbi.1993.1439

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fvl"

@@ Line 1: / Line 1: @@
 ==THE NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF FLAVORIDIN, AN ANTAGONIST OF THE PLATELET GP IIB-IIIA RECEPTOR==
-<StructureSection load='1fvl' size='340' side='right' caption='[[1fvl]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
+<StructureSection load='1fvl' size='340' side='right'caption='[[1fvl]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1fvl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trimeresurus_flavoviridis Trimeresurus 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FVL FirstGlance]. <br>
@@ Line 12: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/1fvl_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/1fvl_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 31: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Trimeresurus flavoviridis]]
 [[Category: Klaus, W]]

1fvl

From Proteopedia

Revision as of 07:36, 19 June 2019

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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