2mbx

From Proteopedia

(Difference between revisions)

Revision as of 11:34, 16 February 2022

Structure, dynamics and stability of allergen cod parvalbumin Gad m 1 by solution and high-pressure NMR.

Structural highlights

2mbx is a 1 chain structure with sequence from Atlantic cod. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRVB_GADMO] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions (By similarity).

Publication Abstract from PubMed

Beta-parvalbumins from different fish species have been identified as the main elicitors of IgE-mediated reactions in fish-allergic individuals. Here, we report for the first time the NMR determination of the structure and dynamics of the major Atlantic cod (Gadus morhua) allergen Gad m 1 and compare them with other known parvalbumins. Although the Gad m 1 structure and accessibility of putative IgE epitopes are similar to parvalbumins in mackerel and carp, the charge distribution at the putative epitopes is different. The determination of the Gad m 1 structure contributes to a better understanding of cross-reactivity among fish parvalbumins. In addition, the high-pressure NMR and temperature variation experiments revealed the important contribution of the AB motif and other regions to the protein folding. This structural information could assist the future identification of hot spots for targeted mutations to develop hypoallergenic Ca(2+) -free forms for potential use in immunotherapy. Proteins 2014; 82:3032-3042. (c) 2014 Wiley Periodicals, Inc.

Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1.,Moraes AH, Ackerbauer D, Kostadinova M, Bublin M, de Oliveira GA, Ferreira F, Almeida FC, Breiteneder H, Valente AP Proteins. 2014 Nov;82(11):3032-42. doi: 10.1002/prot.24664. Epub 2014 Aug 30. PMID:25116395^[1]

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

References

↑ Moraes AH, Ackerbauer D, Kostadinova M, Bublin M, de Oliveira GA, Ferreira F, Almeida FC, Breiteneder H, Valente AP. Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1. Proteins. 2014 Nov;82(11):3032-42. doi: 10.1002/prot.24664. Epub 2014 Aug 30. PMID:25116395 doi:http://dx.doi.org/10.1002/prot.24664

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mbx"

@@ Line 3: / Line 3: @@
 <StructureSection load='2mbx' size='340' side='right'caption='[[2mbx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2mbx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atlantic_cod Atlantic cod]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2MBX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2mbx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atlantic_cod Atlantic cod]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MBX FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2mbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbx OCA], [http://pdbe.org/2mbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mbx RCSB], [http://www.ebi.ac.uk/pdbsum/2mbx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbx ProSAT]</span></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=2mbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbx OCA], [https://pdbe.org/2mbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mbx RCSB], [https://www.ebi.ac.uk/pdbsum/2mbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PRVB_GADMO PRVB_GADMO]] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions (By similarity).
+[[https://www.uniprot.org/uniprot/PRVB_GADMO PRVB_GADMO]] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2mbx

From Proteopedia

Revision as of 11:34, 16 February 2022

Structure, dynamics and stability of allergen cod parvalbumin Gad m 1 by solution and high-pressure NMR.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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