1e4s: Difference between revisions

Line 1:

~~{{STRUCTURE_1e4s| PDB=1e4s | SCENE= }}~~

==SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-1==

===SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-1===

~~{{ABSTRACT_PUBMED_11714914}}~~

== Structural highlights ==

<table><tr><td colspan='2'>[[1e4s]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E4S FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e4s RCSB], [http://www.ebi.ac.uk/pdbsum/1e4s PDBsum]</span></td></tr>

<table>

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/1e4s_consurf.spt"</scriptWhenChecked>

<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/chain_selection.php?pdb_ID=2ata ConSurf].

== Publication Abstract from PubMed ==

Defensins are cationic and cysteine-rich peptides that play a crucial role in the host defense against microorganisms of many organisms by their capability to permeabilize bacterial membranes. The low sequence similarity among the members of the large mammalian beta-defensin family suggests that their antimicrobial activity is largely independent of their primary structure. To investigate to what extent these defensins share a similar fold, the structures of the two human beta-defensins, hBD-1 and hBD-2, as well as those of two novel murine defensins, termed mBD-7 and mBD-8, were determined by nuclear magnetic resonance spectroscopy. All four defensins investigated share a striking similarity on the level of secondary and tertiary structure including the lack of a distinct hydrophobic core, suggesting that the fold is mainly stabilized by the presence of three disulfide bonds. In addition to the overall shape of the molecules, the ratio of solvent-exposed polar and hydrophobic side chains is also very similar among the four defensins investigated. It is significant that beta-defensins do not exhibit a common pattern of charged and hydrophobic residues on the protein surface and that the beta-defensin-specific fold appears to accommodate a wide range of different amino acids at most sequence positions. In addition to the implications for the mode of biological defensin actions, these findings are of particular interest because beta-defensins have been suggested as lead compounds for the development of novel peptide antibiotics for the therapy of infectious diseases.

~~==About this~~ Structure==

Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity.,Bauer F, Schweimer K, Kluver E, Conejo-Garcia JR, Forssmann WG, Rosch P, Adermann K, Sticht H Protein Sci. 2001 Dec;10(12):2470-9. PMID:11714914<ref>PMID:11714914</ref>

~~[[1e4s]] is a 1 chain structure~~. ~~Full experimental information is available from [http~~://~~oca~~.~~weizmann~~.ac.~~il/oca-bin~~/~~ocashort?id=1E4S OCA].~~

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

</div>

==See Also==

*[[Defensin|Defensin]]

== References ==

==~~Reference~~==

<~~ref group="xtra">PMID:011714914<~~/~~ref~~><~~references group="xtra"~~/>

__TOC__

</StructureSection>

[[Category: Adermann, K.]]

[[Category: Bauer, F.]]

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_1e4s|  PDB=1e4s  |  SCENE=  }}
+==SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-1==
-===SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-1===
+<StructureSection load='1e4s' size='340' side='right' caption='[[1e4s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
-{{ABSTRACT_PUBMED_11714914}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1e4s]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E4S FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e4s RCSB], [http://www.ebi.ac.uk/pdbsum/1e4s PDBsum]</span></td></tr>
+<table>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/1e4s_consurf.spt"</scriptWhenChecked>
+    <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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Defensins are cationic and cysteine-rich peptides that play a crucial role in the host defense against microorganisms of many organisms by their capability to permeabilize bacterial membranes. The low sequence similarity among the members of the large mammalian beta-defensin family suggests that their antimicrobial activity is largely independent of their primary structure. To investigate to what extent these defensins share a similar fold, the structures of the two human beta-defensins, hBD-1 and hBD-2, as well as those of two novel murine defensins, termed mBD-7 and mBD-8, were determined by nuclear magnetic resonance spectroscopy. All four defensins investigated share a striking similarity on the level of secondary and tertiary structure including the lack of a distinct hydrophobic core, suggesting that the fold is mainly stabilized by the presence of three disulfide bonds. In addition to the overall shape of the molecules, the ratio of solvent-exposed polar and hydrophobic side chains is also very similar among the four defensins investigated. It is significant that beta-defensins do not exhibit a common pattern of charged and hydrophobic residues on the protein surface and that the beta-defensin-specific fold appears to accommodate a wide range of different amino acids at most sequence positions. In addition to the implications for the mode of biological defensin actions, these findings are of particular interest because beta-defensins have been suggested as lead compounds for the development of novel peptide antibiotics for the therapy of infectious diseases.
-==About this Structure==
+Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity.,Bauer F, Schweimer K, Kluver E, Conejo-Garcia JR, Forssmann WG, Rosch P, Adermann K, Sticht H Protein Sci. 2001 Dec;10(12):2470-9. PMID:11714914<ref>PMID:11714914</ref>
-[[1e4s]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4S OCA].
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
 ==See Also==
 *[[Defensin|Defensin]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011714914</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Adermann, K.]]
 [[Category: Bauer, F.]]