1sjx

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(New page: 200px<br /> <applet load="1sjx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sjx, resolution 2.20&Aring;" /> '''Three-Dimensional S...)
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<applet load="1sjx" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1sjx, resolution 2.20&Aring;" />
caption="1sjx, resolution 2.20&Aring;" />
'''Three-Dimensional Structure of a Llama VHH Domain OE7 binding the cell wall protein Malf1'''<br />
'''Three-Dimensional Structure of a Llama VHH Domain OE7 binding the cell wall protein Malf1'''<br />
==Overview==
==Overview==
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As part of research exploring the feasibility of using antibody fragments, to inhibit the growth of organisms implicated in dandruff, we isolated, antibody fragments that bind to a cell surface protein of Malassezia, furfur in the presence of shampoo. We found that phage display of llama, single-domain antibody fragments (VHHs) can be extended to very harsh, conditions, such as the presence of shampoo containing nonionic and, anionic surfactants. We selected several VHHs that bind to the cell wall, protein Malf1 of M. furfur, a fungus implicated in causing dandruff. In, addition to high stability in the presence of shampoo, these VHHs are also, stable under other denaturing conditions, such as high urea, concentrations. Many of the stable VHHs were found to contain arginine at, position 44. Replacement of the native amino acid at position 44 with, arginine in the most stable VHH that lacked this arginine resulted in a, dramatic further increase in the stability. The combination of the unique, properties of VHHs together with applied phage display and protein, engineering is a powerful method for obtaining highly stable VHHs that can, be used in a wide range of applications.
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As part of research exploring the feasibility of using antibody fragments to inhibit the growth of organisms implicated in dandruff, we isolated antibody fragments that bind to a cell surface protein of Malassezia furfur in the presence of shampoo. We found that phage display of llama single-domain antibody fragments (VHHs) can be extended to very harsh conditions, such as the presence of shampoo containing nonionic and anionic surfactants. We selected several VHHs that bind to the cell wall protein Malf1 of M. furfur, a fungus implicated in causing dandruff. In addition to high stability in the presence of shampoo, these VHHs are also stable under other denaturing conditions, such as high urea concentrations. Many of the stable VHHs were found to contain arginine at position 44. Replacement of the native amino acid at position 44 with arginine in the most stable VHH that lacked this arginine resulted in a dramatic further increase in the stability. The combination of the unique properties of VHHs together with applied phage display and protein engineering is a powerful method for obtaining highly stable VHHs that can be used in a wide range of applications.
==About this Structure==
==About this Structure==
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1SJX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Limia Limia] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SJX OCA].
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1SJX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Limia Limia] with <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJX OCA].
==Reference==
==Reference==
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[[Category: Dolk, E.]]
[[Category: Dolk, E.]]
[[Category: Frenken, L.]]
[[Category: Frenken, L.]]
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[[Category: Haard, H.de.]]
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[[Category: Haard, H de.]]
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[[Category: Hulsik, D.L.]]
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[[Category: Hulsik, D L.]]
[[Category: Spinelli, S.]]
[[Category: Spinelli, S.]]
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[[Category: Vaart, M.van.der.]]
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[[Category: Vaart, M van der.]]
[[Category: Verrips, T.]]
[[Category: Verrips, T.]]
[[Category: Vriend, G.]]
[[Category: Vriend, G.]]
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[[Category: phage display]]
[[Category: phage display]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:42:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:14 2008''

Revision as of 13:02, 21 February 2008


1sjx, resolution 2.20Å

Drag the structure with the mouse to rotate

Three-Dimensional Structure of a Llama VHH Domain OE7 binding the cell wall protein Malf1

Overview

As part of research exploring the feasibility of using antibody fragments to inhibit the growth of organisms implicated in dandruff, we isolated antibody fragments that bind to a cell surface protein of Malassezia furfur in the presence of shampoo. We found that phage display of llama single-domain antibody fragments (VHHs) can be extended to very harsh conditions, such as the presence of shampoo containing nonionic and anionic surfactants. We selected several VHHs that bind to the cell wall protein Malf1 of M. furfur, a fungus implicated in causing dandruff. In addition to high stability in the presence of shampoo, these VHHs are also stable under other denaturing conditions, such as high urea concentrations. Many of the stable VHHs were found to contain arginine at position 44. Replacement of the native amino acid at position 44 with arginine in the most stable VHH that lacked this arginine resulted in a dramatic further increase in the stability. The combination of the unique properties of VHHs together with applied phage display and protein engineering is a powerful method for obtaining highly stable VHHs that can be used in a wide range of applications.

About this Structure

1SJX is a Protein complex structure of sequences from Limia with as ligand. Full crystallographic information is available from OCA.

Reference

Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo., Dolk E, van der Vaart M, Lutje Hulsik D, Vriend G, de Haard H, Spinelli S, Cambillau C, Frenken L, Verrips T, Appl Environ Microbiol. 2005 Jan;71(1):442-50. PMID:15640220

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