1lyp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1lyp" [edit=sysop:move=sysop])
Current revision (18:48, 29 November 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lyp.png|left|200px]]
 
-
{{STRUCTURE_1lyp| PDB=1lyp | SCENE= }}
+
==THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTES==
 +
<StructureSection load='1lyp' size='340' side='right'caption='[[1lyp]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1lyp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LYP FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1lyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lyp OCA], [https://pdbe.org/1lyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lyp RCSB], [https://www.ebi.ac.uk/pdbsum/1lyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lyp ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CAP18_RABIT CAP18_RABIT] CAP18 binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Has antibiotic activity.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
We have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18(106-137), a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18(106-137) may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18(106-137) in 30% (v/v) TFE, determined by nuclear magnetic resonance (NMR) technique, was found to be a complete and very rigid helix. In this conformation, the cationic and hydrophobic groups of CAP18(106-137) are separated into patches and stripes in such a way that it can favorably interact with lipid A through either coulombic interaction with the diphosphoryl groups or hydrophobic interaction with the fatty acyl chains.
-
===THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTES===
+
The solution structure of the active domain of CAP18--a lipopolysaccharide binding protein from rabbit leukocytes.,Chen C, Brock R, Luh F, Chou PJ, Larrick JW, Huang RF, Huang TH FEBS Lett. 1995 Aug 14;370(1-2):46-52. PMID:7649303<ref>PMID:7649303</ref>
-
{{ABSTRACT_PUBMED_7649303}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 1lyp" style="background-color:#fffaf0;"></div>
-
[[1lyp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYP OCA].
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Chen, C.]]
+
[[Category: Chen C]]
-
[[Category: Huang, T H.]]
+
[[Category: Huang T-H]]
-
[[Category: Lipopolysaccharide-binding protein]]
+

Current revision

THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTES

PDB ID 1lyp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools