1bfb: Difference between revisions

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[[Image:1bfb.gif|left|200px]]<br />

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

<applet load="1bfb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1bfb, resolution 1.9Å" />

'''BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN TETRAMER FRAGMENT'''<br />

==Overview==

Crystal structures of heparin-derived tetra- and hexasaccharides complexed, with basic fibroblast growth factor (bFGF) were determined at resolutions, of 1.9 and 2.2 angstroms, respectively. The heparin structure may be, approximated as a helical polymer with a disaccharide rotation of 174, degrees and a translation of 8.6 angstroms along the helix axis. Both, molecules bound similarly to a region of the bFGF surface containing, residues asparagine-28, arginine-121, lysine-126, and glutamine-135, the, hexasaccharide also interacted with an additional binding site formed by, lysine-27, asparagine-102, and lysine-136. No significant conformational, change in bFGF occurred upon heparin oligosaccharide binding, which, suggests that heparin primarily serves to juxtapose components of the FGF, signal transduction pathway.

Crystal structures of heparin-derived tetra- and hexasaccharides complexed with basic fibroblast growth factor (bFGF) were determined at resolutions of 1.9 and 2.2 angstroms, respectively. The heparin structure may be approximated as a helical polymer with a disaccharide rotation of 174 degrees and a translation of 8.6 angstroms along the helix axis. Both molecules bound similarly to a region of the bFGF surface containing residues asparagine-28, arginine-121, lysine-126, and glutamine-135, the hexasaccharide also interacted with an additional binding site formed by lysine-27, asparagine-102, and lysine-136. No significant conformational change in bFGF occurred upon heparin oligosaccharide binding, which suggests that heparin primarily serves to juxtapose components of the FGF signal transduction pathway.

==Disease==

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==About this Structure==

1BFB 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=1BFB OCA].

1BFB 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=1BFB OCA].

==Reference==

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[[Category: Single protein]]

[[Category: Faham, S.]]

[[Category: Rees, D.C.]]

[[Category: Rees, D C.]]

[[Category: growth factor]]

[[Category: heparin-binding]]

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[[Category: vascularization]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 16~~:09:~~09 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:41 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1bfb.gif|left|200px]]<br />
+[[Image:1bfb.gif|left|200px]]<br /><applet load="1bfb" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1bfb" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1bfb, resolution 1.9&Aring;" />
 '''BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN TETRAMER FRAGMENT'''<br />
 ==Overview==
-Crystal structures of heparin-derived tetra- and hexasaccharides complexed, with basic fibroblast growth factor (bFGF) were determined at resolutions, of 1.9 and 2.2 angstroms, respectively. The heparin structure may be, approximated as a helical polymer with a disaccharide rotation of 174, degrees and a translation of 8.6 angstroms along the helix axis. Both, molecules bound similarly to a region of the bFGF surface containing, residues asparagine-28, arginine-121, lysine-126, and glutamine-135, the, hexasaccharide also interacted with an additional binding site formed by, lysine-27, asparagine-102, and lysine-136. No significant conformational, change in bFGF occurred upon heparin oligosaccharide binding, which, suggests that heparin primarily serves to juxtapose components of the FGF, signal transduction pathway.
+Crystal structures of heparin-derived tetra- and hexasaccharides complexed with basic fibroblast growth factor (bFGF) were determined at resolutions of 1.9 and 2.2 angstroms, respectively. The heparin structure may be approximated as a helical polymer with a disaccharide rotation of 174 degrees and a translation of 8.6 angstroms along the helix axis. Both molecules bound similarly to a region of the bFGF surface containing residues asparagine-28, arginine-121, lysine-126, and glutamine-135, the hexasaccharide also interacted with an additional binding site formed by lysine-27, asparagine-102, and lysine-136. No significant conformational change in bFGF occurred upon heparin oligosaccharide binding, which suggests that heparin primarily serves to juxtapose components of the FGF signal transduction pathway.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-BFB 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=1BFB OCA].
+BFB 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=1BFB OCA].
 ==Reference==
@@ Line 18: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Faham, S.]]
-[[Category: Rees, D.C.]]
+[[Category: Rees, D C.]]
 [[Category: growth factor]]
 [[Category: heparin-binding]]
@@ Line 24: / Line 23: @@
 [[Category: vascularization]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:09:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:41 2008''