2mit: Difference between revisions

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'''Unreleased structure'''
==Solution structure of oxidized dimeric form of human defensin 5==
 
<StructureSection load='2mit' size='340' side='right' caption='[[2mit]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
The entry 2mit is ON HOLD  until sometime in the future
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2mit]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MIT FirstGlance]. <br>
Authors: Wommack, A.J., Ziarek, J.J., Wagner, G., Nolan, E.M.
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lxz|2lxz]], [[1zmp|1zmp]]</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mit RCSB], [http://www.ebi.ac.uk/pdbsum/2mit PDBsum]</span></td></tr>
Description: Solution structure of oxidized dimeric form of human defensin 5
</table>
== Function ==
[[http://www.uniprot.org/uniprot/DEF5_HUMAN DEF5_HUMAN]] Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing.<ref>PMID:12021776</ref> <ref>PMID:15616305</ref> <ref>PMID:17088326</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Nolan, E M]]
[[Category: Wagner, G]]
[[Category: Wommack, A J]]
[[Category: Ziarek, J J]]
[[Category: Antimicrobial peptide]]
[[Category: Antimicrobial protein]]
[[Category: Cysteine knot]]

Revision as of 16:12, 5 January 2015

Solution structure of oxidized dimeric form of human defensin 5Solution structure of oxidized dimeric form of human defensin 5

Structural highlights

2mit is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[DEF5_HUMAN] Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing.[1] [2] [3]

References

  1. ↑ Ghosh D, Porter E, Shen B, Lee SK, Wilk D, Drazba J, Yadav SP, Crabb JW, Ganz T, Bevins CL. Paneth cell trypsin is the processing enzyme for human defensin-5. Nat Immunol. 2002 Jun;3(6):583-90. Epub 2002 May 20. PMID:12021776 doi:10.1038/ni797
  2. ↑ Ericksen B, Wu Z, Lu W, Lehrer RI. Antibacterial activity and specificity of the six human {alpha}-defensins. Antimicrob Agents Chemother. 2005 Jan;49(1):269-75. PMID:15616305 doi:10.1128/AAC.49.1.269-275.2005
  3. ↑ Szyk A, Wu Z, Tucker K, Yang D, Lu W, Lubkowski J. Crystal structures of human alpha-defensins HNP4, HD5, and HD6. Protein Sci. 2006 Dec;15(12):2749-60. Epub 2006 Nov 6. PMID:17088326 doi:ps.062336606
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