6nom: Difference between revisions
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New page: '''Unreleased structure''' The entry 6nom is ON HOLD Authors: Description: Category: Unreleased Structures |
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==NMR solution structure of Pisum sativum defensin 2 (Psd2) provides evidence for the presence of hydrophobic surface clusters== | |||
<StructureSection load='6nom' size='340' side='right'caption='[[6nom]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6nom]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NOM FirstGlance]. <br> | |||
</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=6nom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nom OCA], [https://pdbe.org/6nom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nom RCSB], [https://www.ebi.ac.uk/pdbsum/6nom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nom ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DEF2_PEA DEF2_PEA] Possesses antifungal activity sensitive to inorganic cations. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pisum sativum defensin 2 (Psd2) is a small (4.7 kDa) antifungal peptide whose structure is held together by four conserved disulfide bridges. Psd2 shares the cysteine-stabilized alpha-beta (CSalphabeta) fold, which lacks a regular hydrophobic core. All hydrophobic residues are exposed to the surface, except for leucine 6. They are clustered in the surface formed by two loops, between beta1 and alpha-helix and beta2 and beta3 sheets. The observation of surface hydrophobic clusters reveals a remarkable evolution of the CSalphabeta fold to expose and reorganize hydrophobic residues, which facilitates creating versatile binding sites. | |||
Nuclear magnetic resonance solution structure of Pisum sativum defensin 2 provides evidence for the presence of hydrophobic surface-clusters.,Pinheiro-Aguiar R, do Amaral VSG, Pereira IB, Kurtenbach E, Almeida FCL Proteins. 2019 Jul 11. doi: 10.1002/prot.25783. PMID:31294889<ref>PMID:31294889</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6nom" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Defensin 3D structures|Defensin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pisum sativum]] | |||
[[Category: Almeida FCL]] | |||
[[Category: Amaral VSG]] | |||
[[Category: Bastos I]] | |||
[[Category: Kurtenbach E]] | |||
[[Category: Pinheiro-Aguiar R]] | |||
Latest revision as of 13:15, 23 October 2024
NMR solution structure of Pisum sativum defensin 2 (Psd2) provides evidence for the presence of hydrophobic surface clustersNMR solution structure of Pisum sativum defensin 2 (Psd2) provides evidence for the presence of hydrophobic surface clusters
Structural highlights
FunctionDEF2_PEA Possesses antifungal activity sensitive to inorganic cations. Publication Abstract from PubMedPisum sativum defensin 2 (Psd2) is a small (4.7 kDa) antifungal peptide whose structure is held together by four conserved disulfide bridges. Psd2 shares the cysteine-stabilized alpha-beta (CSalphabeta) fold, which lacks a regular hydrophobic core. All hydrophobic residues are exposed to the surface, except for leucine 6. They are clustered in the surface formed by two loops, between beta1 and alpha-helix and beta2 and beta3 sheets. The observation of surface hydrophobic clusters reveals a remarkable evolution of the CSalphabeta fold to expose and reorganize hydrophobic residues, which facilitates creating versatile binding sites. Nuclear magnetic resonance solution structure of Pisum sativum defensin 2 provides evidence for the presence of hydrophobic surface-clusters.,Pinheiro-Aguiar R, do Amaral VSG, Pereira IB, Kurtenbach E, Almeida FCL Proteins. 2019 Jul 11. doi: 10.1002/prot.25783. PMID:31294889[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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