2bbx

From Proteopedia

(Difference between revisions)

Current revision

NMR solution structure of the TSR domain of malaria TRAP protein

Structural highlights

2bbx is a 1 chain structure with sequence from Plasmodium falciparum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRAP_PLAFA

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

Thrombospondin-related anonymous protein, TRAP, has a critical role in the hepatocyte invasion step of Plasmodium sporozoites, the transmissible form of the parasite causing malaria. The extracellular domains of this sporozoite surface protein interact with hepatocyte surface receptors whereas its intracellular domain acts as a link to the sporozoite actomyosin motor system. Liver heparan sulfate proteoglycans have been identified as potential ligands for TRAP. Proteoglycan binding has been associated with the A- and TSR domains of TRAP. We present the solution NMR structure of the TSR domain of TRAP and a chemical shift mapping study of its heparin binding epitope. The domain has an elongated structure stabilized by an array of tryptophan and arginine residues as well as disulfide bonds. The fold is very similar to those of thrombospondin type-1 (TSP-1) and F-spondin TSRs. The heparin binding site of TRAP-TSR is located in the N-terminal half of the structure, the layered side chains forming an integral part of the site. The smallest heparin fragment capable of binding to TRAP-TSR is a tetrasaccharide.

The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site.,Tossavainen H, Pihlajamaa T, Huttunen TK, Raulo E, Rauvala H, Permi P, Kilpelainen I Protein Sci. 2006 Jul;15(7):1760-8. PMID:16815922^[1]

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

References

↑ Tossavainen H, Pihlajamaa T, Huttunen TK, Raulo E, Rauvala H, Permi P, Kilpelainen I. The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site. Protein Sci. 2006 Jul;15(7):1760-8. PMID:16815922 doi:15/7/1760

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/2bbx"

Categories: Large Structures | Plasmodium falciparum | Kilpelainen I | Permi P | Tossavainen H

@@ Line 1: / Line 1: @@
 ==NMR solution structure of the TSR domain of malaria TRAP protein==
-<StructureSection load='2bbx' size='340' side='right'caption='[[2bbx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2bbx' size='340' side='right'caption='[[2bbx]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bbx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plafa Plafa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BBX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bbx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BBX FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRAP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 PLAFA])</td></tr>
+</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=2bbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bbx OCA], [https://pdbe.org/2bbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bbx RCSB], [https://www.ebi.ac.uk/pdbsum/2bbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bbx ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRAP_PLAFA TRAP_PLAFA]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 12: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bb/2bbx_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Plafa]]
+[[Category: Plasmodium falciparum]]
-[[Category: Kilpelainen, I]]
+[[Category: Kilpelainen I]]
-[[Category: Permi, P]]
+[[Category: Permi P]]
-[[Category: Tossavainen, H]]
+[[Category: Tossavainen H]]
-[[Category: Cell adhesion]]
-[[Category: Elongated three-stranded structure]]

2bbx

From Proteopedia

Current revision

NMR solution structure of the TSR domain of malaria TRAP protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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