2ila: Difference between revisions

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[[Image:2ila.gif|left|200px]]<br />

[[Image:2ila.gif|left|200px]]<br /><applet load="2ila" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2ila" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2ila, resolution 2.3Å" />

'''STRUCTURE OF INTERLEUKIN 1ALPHA AT 2.7-ANGSTROMS RESOLUTION'''<br />

==Overview==

The interleukin 1 (IL-1) family of proteins has a central role in, modulating immune and inflammatory responses. Two major IL-1 proteins, designated alpha (IL-1 alpha) and beta (IL-1 beta), are produced by, activated macrophages and other cell types. In an effort to understand the, similarities and differences in the physicochemical and functional, properties of these two proteins, a program was initiated to determine, their structures. Crystals of IL-1 alpha were grown, and the, three-dimensional structure at 2.7-A resolution was solved. The technique, of multiple-wavelength anomalous dispersion (MAD) with the, selenomethionine form of IL-1 alpha was utilized in combination with a, single mercury derivative to provide the starting phases. Partial, refinement of the IL-1 alpha model has been performed as well. The overall, structure is composed of 14 beta-strands and a 3(10) helix. The core of, this structure is a capped beta-barrell that possesses 3-fold symmetry and, displays a topology similar to that observed for IL-1 beta [Priestle, J., P., et al. (1988) EMBO J. 7, 339-343] and soybean trypsin inhibitor (STI), [McLachlan, A. D. (1979) J. Mol. Biol. 133, 557-563]. In this paper, the, overall structure of IL-1 alpha and the nature and fidelity of the, internal 3-fold symmetry are discussed. Comparisons with IL-1 beta and STI, are made within these contexts.

The interleukin 1 (IL-1) family of proteins has a central role in modulating immune and inflammatory responses. Two major IL-1 proteins, designated alpha (IL-1 alpha) and beta (IL-1 beta), are produced by activated macrophages and other cell types. In an effort to understand the similarities and differences in the physicochemical and functional properties of these two proteins, a program was initiated to determine their structures. Crystals of IL-1 alpha were grown, and the three-dimensional structure at 2.7-A resolution was solved. The technique of multiple-wavelength anomalous dispersion (MAD) with the selenomethionine form of IL-1 alpha was utilized in combination with a single mercury derivative to provide the starting phases. Partial refinement of the IL-1 alpha model has been performed as well. The overall structure is composed of 14 beta-strands and a 3(10) helix. The core of this structure is a capped beta-barrell that possesses 3-fold symmetry and displays a topology similar to that observed for IL-1 beta [Priestle, J. P., et al. (1988) EMBO J. 7, 339-343] and soybean trypsin inhibitor (STI) [McLachlan, A. D. (1979) J. Mol. Biol. 133, 557-563]. In this paper, the overall structure of IL-1 alpha and the nature and fidelity of the internal 3-fold symmetry are discussed. Comparisons with IL-1 beta and STI are made within these contexts.

==About this Structure==

2ILA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2ILA OCA].

2ILA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILA OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Graves, B.J.]]

[[Category: Graves, B J.]]

[[Category: Hatada, M.H.]]

[[Category: Hatada, M H.]]

[[Category: cytokine]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:45:~~38 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:53:47 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2ila.gif|left|200px]]<br />
+[[Image:2ila.gif|left|200px]]<br /><applet load="2ila" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2ila" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2ila, resolution 2.3&Aring;" />
 '''STRUCTURE OF INTERLEUKIN 1ALPHA AT 2.7-ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-The interleukin 1 (IL-1) family of proteins has a central role in, modulating immune and inflammatory responses. Two major IL-1 proteins, designated alpha (IL-1 alpha) and beta (IL-1 beta), are produced by, activated macrophages and other cell types. In an effort to understand the, similarities and differences in the physicochemical and functional, properties of these two proteins, a program was initiated to determine, their structures. Crystals of IL-1 alpha were grown, and the, three-dimensional structure at 2.7-A resolution was solved. The technique, of multiple-wavelength anomalous dispersion (MAD) with the, selenomethionine form of IL-1 alpha was utilized in combination with a, single mercury derivative to provide the starting phases. Partial, refinement of the IL-1 alpha model has been performed as well. The overall, structure is composed of 14 beta-strands and a 3(10) helix. The core of, this structure is a capped beta-barrell that possesses 3-fold symmetry and, displays a topology similar to that observed for IL-1 beta [Priestle, J., P., et al. (1988) EMBO J. 7, 339-343] and soybean trypsin inhibitor (STI), [McLachlan, A. D. (1979) J. Mol. Biol. 133, 557-563]. In this paper, the, overall structure of IL-1 alpha and the nature and fidelity of the, internal 3-fold symmetry are discussed. Comparisons with IL-1 beta and STI, are made within these contexts.
+The interleukin 1 (IL-1) family of proteins has a central role in modulating immune and inflammatory responses. Two major IL-1 proteins, designated alpha (IL-1 alpha) and beta (IL-1 beta), are produced by activated macrophages and other cell types. In an effort to understand the similarities and differences in the physicochemical and functional properties of these two proteins, a program was initiated to determine their structures. Crystals of IL-1 alpha were grown, and the three-dimensional structure at 2.7-A resolution was solved. The technique of multiple-wavelength anomalous dispersion (MAD) with the selenomethionine form of IL-1 alpha was utilized in combination with a single mercury derivative to provide the starting phases. Partial refinement of the IL-1 alpha model has been performed as well. The overall structure is composed of 14 beta-strands and a 3(10) helix. The core of this structure is a capped beta-barrell that possesses 3-fold symmetry and displays a topology similar to that observed for IL-1 beta [Priestle, J. P., et al. (1988) EMBO J. 7, 339-343] and soybean trypsin inhibitor (STI) [McLachlan, A. D. (1979) J. Mol. Biol. 133, 557-563]. In this paper, the overall structure of IL-1 alpha and the nature and fidelity of the internal 3-fold symmetry are discussed. Comparisons with IL-1 beta and STI are made within these contexts.
 ==About this Structure==
-ILA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ILA OCA].
+ILA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILA OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Graves, B.J.]]
+[[Category: Graves, B J.]]
-[[Category: Hatada, M.H.]]
+[[Category: Hatada, M H.]]
 [[Category: cytokine]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:45:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:53:47 2008''