1lyp: Difference between revisions

Revision as of 22:50, 2 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:1lyp.png

Template:STRUCTURE 1lyp

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

Template:ABSTRACT PUBMED 7649303

About this StructureAbout this Structure

1LYP is a Single protein structure of sequence from Oryctolagus cuniculus. Full experimental information is available from OCA.

ReferenceReference

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

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

OCA

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-'''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===
-==Overview==
+<!--
-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 line below this paragraph, {{ABSTRACT_PUBMED_7649303}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7649303 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7649303}}
 ==About this Structure==
-LYP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYP OCA].
+LYP is a [[Single protein]] structure of 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].
 ==Reference==
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 [[Category: Huang, T H.]]
 [[Category: Lipopolysaccharide-binding protein]]
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