1lyp: Difference between revisions

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[[Image:1lyp.jpg|left|200px]]<br /><applet load="1lyp" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1lyp.jpg|left|200px]]<br /><applet load="1lyp" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1lyp" />

'''THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTES'''<br />

==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.

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.

==About this Structure==

1LYP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1LYP OCA].

1LYP is a [http://en.wikipedia.org/wiki/Single_protein 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].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Chen, C.]]

[[Category: Huang, T.H.]]

[[Category: Huang, T H.]]

[[Category: lipopolysaccharide-binding protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 20~~:59:~~39 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:40 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1lyp.jpg|left|200px]]<br /><applet load="1lyp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1lyp.jpg|left|200px]]<br /><applet load="1lyp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1lyp" />
 '''THE SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF CAP18: A LIPOPOLYSACCHARIDE BINDING PROTEIN FROM RABBIT LEUKOCYTES'''<br />
 ==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.
+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.
 ==About this Structure==
-LYP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LYP OCA].
+LYP is a [http://en.wikipedia.org/wiki/Single_protein 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].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Chen, C.]]
-[[Category: Huang, T.H.]]
+[[Category: Huang, T H.]]
 [[Category: lipopolysaccharide-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:59:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:40 2008''