1fqq: Difference between revisions

Revision as of 03:47, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fqq.png

Template:STRUCTURE 1fqq

SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN-2SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN-2

Template:ABSTRACT PUBMED 11300761

About this StructureAbout this Structure

1FQQ is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 03:47:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1fqq.gif|left|200px]]
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 {{STRUCTURE_1fqq|  PDB=1fqq  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN-2'''
+===SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN-2===
-==Overview==
+<!--
-Human 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 &lt; 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 line below this paragraph, {{ABSTRACT_PUBMED_11300761}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11300761 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11300761}}
 ==About this Structure==
-FQQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQQ OCA].
+FQQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQQ OCA].
 ==Reference==
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 [[Category: Defensin]]
 [[Category: Solution structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:39:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:47:54 2008''