1fqq: Difference between revisions
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<StructureSection load='1fqq' size='340' side='right' caption='[[1fqq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1fqq' size='340' side='right' caption='[[1fqq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fqq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1fqq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FQQ FirstGlance]. <br> | ||
</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=1fqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fqq RCSB], [http://www.ebi.ac.uk/pdbsum/1fqq PDBsum]</span></td></tr> | </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=1fqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqq OCA], [http://pdbe.org/1fqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fqq RCSB], [http://www.ebi.ac.uk/pdbsum/1fqq PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1fqq" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Aseyev, V]] | [[Category: Aseyev, V]] | ||
[[Category: Ganz, T]] | [[Category: Ganz, T]] | ||
Revision as of 02:05, 10 September 2015
SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN-2SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN-2
Structural highlights
Publication Abstract from PubMedHuman beta-defensin-2 (HBD-2) is a member of the defensin family of antimicrobial peptides. HBD-2 was first isolated from inflamed skin where it is posited to participate in the killing of invasive bacteria and in the recruitment of cells of the adaptive immune response. Static light scattering and two-dimensional proton nuclear magnetic resonance spectroscopy have been used to assess the physical state and structure of HBD-2 in solution. At concentrations of < or = 2.4 mM, HBD-2 is monomeric. The structure is amphiphilic with a nonuniform surface distribution of positive charge and contains several key structural elements, including a triple-stranded, antiparallel beta-sheet with strands 2 and 3 in a beta-hairpin conformation. A beta-bulge in the second strand occurs at Gly28, a position conserved in the entire defensin family. In solution, HBD-2 exhibits an alpha-helical segment near the N-terminus that has not been previously ascribed to solution structures of alpha-defensins or to the beta-defensin BNBD-12. This novel structural element may be a factor contributing to the specific microbicidal or chemokine-like properties of HBD-2. The NMR structure of human beta-defensin-2 reveals a novel alpha-helical segment.,Sawai MV, Jia HP, Liu L, Aseyev V, Wiencek JM, McCray PB Jr, Ganz T, Kearney WR, Tack BF Biochemistry. 2001 Apr 3;40(13):3810-6. PMID:11300761[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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