2fgf: Difference between revisions

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

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

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

caption="2fgf, resolution 1.77Å" />

'''THREE-DIMENSIONAL STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR, A STRUCTURAL HOMOLOG OF INTERLEUKIN 1BETA'''<br />

==Overview==

The three-dimensional structure of the 146-residue form of human basic, fibroblast growth factor (bFGF), expressed as a recombinant protein in, yeast, has been determined by x-ray crystallography to a resolution of 1.8, A. bFGF is composed entirely of beta-sheet structure, comprising a, three-fold repeat of a four-stranded antiparallel beta-meander. The, topology of bFGF is identical to that of interleukin 1 beta, showing that, although the two proteins share only 10% sequence identity, bFGF, interleukin 1, and their homologs comprise a family of structurally, related mitogenic factors. Analysis of the three-dimensional structure in, light of functional studies of bFGF suggests that the receptor binding, site and the positively charged heparin binding site correspond to, adjacent but separate loci on the beta-barrel.

The three-dimensional structure of the 146-residue form of human basic fibroblast growth factor (bFGF), expressed as a recombinant protein in yeast, has been determined by x-ray crystallography to a resolution of 1.8 A. bFGF is composed entirely of beta-sheet structure, comprising a three-fold repeat of a four-stranded antiparallel beta-meander. The topology of bFGF is identical to that of interleukin 1 beta, showing that although the two proteins share only 10% sequence identity, bFGF, interleukin 1, and their homologs comprise a family of structurally related mitogenic factors. Analysis of the three-dimensional structure in light of functional studies of bFGF suggests that the receptor binding site and the positively charged heparin binding site correspond to adjacent but separate loci on the beta-barrel.

==Disease==

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==About this Structure==

2FGF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2FGF OCA].

2FGF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGF OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Sprang, S.R.]]

[[Category: Sprang, S R.]]

[[Category: Zhang, J.]]

[[Category: SO4]]

[[Category: growth factor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:05~~:02 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:05 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2fgf.gif|left|200px]]<br />
+[[Image:2fgf.gif|left|200px]]<br /><applet load="2fgf" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2fgf" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2fgf, resolution 1.77&Aring;" />
 '''THREE-DIMENSIONAL STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR, A STRUCTURAL HOMOLOG OF INTERLEUKIN 1BETA'''<br />
 ==Overview==
-The three-dimensional structure of the 146-residue form of human basic, fibroblast growth factor (bFGF), expressed as a recombinant protein in, yeast, has been determined by x-ray crystallography to a resolution of 1.8, A. bFGF is composed entirely of beta-sheet structure, comprising a, three-fold repeat of a four-stranded antiparallel beta-meander. The, topology of bFGF is identical to that of interleukin 1 beta, showing that, although the two proteins share only 10% sequence identity, bFGF, interleukin 1, and their homologs comprise a family of structurally, related mitogenic factors. Analysis of the three-dimensional structure in, light of functional studies of bFGF suggests that the receptor binding, site and the positively charged heparin binding site correspond to, adjacent but separate loci on the beta-barrel.
+The three-dimensional structure of the 146-residue form of human basic fibroblast growth factor (bFGF), expressed as a recombinant protein in yeast, has been determined by x-ray crystallography to a resolution of 1.8 A. bFGF is composed entirely of beta-sheet structure, comprising a three-fold repeat of a four-stranded antiparallel beta-meander. The topology of bFGF is identical to that of interleukin 1 beta, showing that although the two proteins share only 10% sequence identity, bFGF, interleukin 1, and their homologs comprise a family of structurally related mitogenic factors. Analysis of the three-dimensional structure in light of functional studies of bFGF suggests that the receptor binding site and the positively charged heparin binding site correspond to adjacent but separate loci on the beta-barrel.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-FGF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FGF OCA].
+FGF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGF OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Sprang, S.R.]]
+[[Category: Sprang, S R.]]
 [[Category: Zhang, J.]]
 [[Category: SO4]]
 [[Category: growth factor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:05:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:05 2008''