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2nls

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Revision as of 15:45, 8 June 2021

Human beta-defensin-1 (Mutant Gln24Ala)

Structural highlights

2nls is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2nlb, 2nlc, 2nld, 2nle, 2nlf, 2nlh, 2nlp, 2nlq
Gene:	DEFB1, BD1, HBD1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DEFB1_HUMAN] Has bactericidal activity (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Defensins are small (30-45 amino acid residues) cationic proteins with broad antimicrobial activity against many bacteria and fungi, some enveloped viruses, and other activities such as chemoattraction of a range of different cell types to the sites of inflammation. These proteins represent attractive targets for developing novel antimicrobial agents and modulators of immune responses with therapeutic applicability. In this report, we present the results of functional and structural studies of 26 single-site mutants of human beta-defensin 1 (hBD1). All mutants were assayed for antimicrobial activity against Escherichia coli (ATCC strain 25922) and for chemotactic activity with CCR6-transfected HEK293 cells. To analyze the structural implications of mutagenesis and to verify the correctness of the disulfide connectivity, we used x-ray crystallography to conduct complete structural studies for 10 mutants in which the topology of disulfides was the same as in the native hBD1. Mutations did not induce significant changes of the tertiary structure, suggesting that the observed alterations of biological properties of the mutants were solely associated with changes in the respective side chains. We found that cationic residues located near the C terminus (Arg(29), Lys(31), Lys(33), and Lys(36)) of hBD1 define most of the anti-E. coli in vitro activity of this protein. In turn, nearly all mutations altering the CCR6-mediated chemotaxis are located at one area of the protein, defined by the N-terminal alpha-helical region (Asp(1)... Ser(8)) and a few topologically adjacent residues (Lys(22), Arg(29), and Lys(33)). These experimental results allow for the first time drafting of the CCR6-epitope for a defensin molecule.

Studies of the biological properties of human beta-defensin 1.,Pazgier M, Prahl A, Hoover DM, Lubkowski J J Biol Chem. 2007 Jan 19;282(3):1819-29. Epub 2006 Oct 27. PMID:17071614^[1]

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

References

↑ Pazgier M, Prahl A, Hoover DM, Lubkowski J. Studies of the biological properties of human beta-defensin 1. J Biol Chem. 2007 Jan 19;282(3):1819-29. Epub 2006 Oct 27. PMID:17071614 doi:http://dx.doi.org/10.1074/jbc.M607210200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nls"

@@ Line 1: / Line 1: @@
 ==Human beta-defensin-1 (Mutant Gln24Ala)==
-<StructureSection load='2nls' size='340' side='right' caption='[[2nls]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
+<StructureSection load='2nls' size='340' side='right'caption='[[2nls]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2nls]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NLS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NLS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2nls]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NLS FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nlb|2nlb]], [[2nlc|2nlc]], [[2nld|2nld]], [[2nle|2nle]], [[2nlf|2nlf]], [[2nlh|2nlh]], [[2nlp|2nlp]], [[2nlq|2nlq]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2nlb|2nlb]], [[2nlc|2nlc]], [[2nld|2nld]], [[2nle|2nle]], [[2nlf|2nlf]], [[2nlh|2nlh]], [[2nlp|2nlp]], [[2nlq|2nlq]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEFB1, BD1, HBD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEFB1, BD1, HBD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2nls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nls OCA], [http://pdbe.org/2nls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nls RCSB], [http://www.ebi.ac.uk/pdbsum/2nls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nls ProSAT]</span></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=2nls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nls OCA], [https://pdbe.org/2nls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nls RCSB], [https://www.ebi.ac.uk/pdbsum/2nls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nls ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DEFB1_HUMAN DEFB1_HUMAN]] Has bactericidal activity (By similarity).
+[[https://www.uniprot.org/uniprot/DEFB1_HUMAN DEFB1_HUMAN]] Has bactericidal activity (By similarity).
 == 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/nl/2nls_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nl/2nls_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 2nls" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Defensin 3D structures|Defensin 3D structures]]
 == References ==
 <references/>
@@ Line 34: / Line 37: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Lubkowski, J]]
 [[Category: Pazgier, M]]

2nls

From Proteopedia

Revision as of 15:45, 8 June 2021

Human beta-defensin-1 (Mutant Gln24Ala)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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