2bfh: Difference between revisions

Line 4:

==Overview==

We have determined the crystal structures of two types of human basic, fibroblast growth factor, the serine analogue and the wild-type, at 1.6, and 2.5 A resolution, respectively. Two good heavy atom derivatives were, found and used for multiple isomorphous replacement phasing. The atomic, coordinates were refined using the Hendrickson & Konnert program for, stereochemically restrained refinement against structure factors. The, crystallographic R factors were reduced to 15.3% for the serine analogue, structure and 16.0% for the wild-type structure. The serine analogue and, wild-type structures have been found to be almost identical, the, root-mean-square deviation between the corresponding C alpha atoms being, 0.11 A. Their structures are composed of twelve beta-strands forming a, barrel and three loops. Their molecules have an approximate threefold, internal symmetry and are similar in architecture to that of interleukin-1, beta. A possible heparin-binding site, which comprises five basic, residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by, calculating the electrostatic potential energy.

We have determined the crystal structures of two types of human basic fibroblast growth factor, the serine analogue and the wild-type, at 1.6 and 2.5 A resolution, respectively. Two good heavy atom derivatives were found and used for multiple isomorphous replacement phasing. The atomic coordinates were refined using the Hendrickson & Konnert program for stereochemically restrained refinement against structure factors. The crystallographic R factors were reduced to 15.3% for the serine analogue structure and 16.0% for the wild-type structure. The serine analogue and wild-type structures have been found to be almost identical, the root-mean-square deviation between the corresponding C alpha atoms being 0.11 A. Their structures are composed of twelve beta-strands forming a barrel and three loops. Their molecules have an approximate threefold internal symmetry and are similar in architecture to that of interleukin-1 beta. A possible heparin-binding site, which comprises five basic residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by calculating the electrostatic potential energy.

==Disease==

Line 13:

==Reference==

Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem ~~(Tokyo)~~. 1991 Sep;110(3):360-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1769963 1769963]

Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem. 1991 Sep;110(3):360-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1769963 1769963]

[[Category: Homo sapiens]]

[[Category: Single protein]]

Line 23:

[[Category: growth factor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 17~~:16:14 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:15 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-We have determined the crystal structures of two types of human basic, fibroblast growth factor, the serine analogue and the wild-type, at 1.6, and 2.5 A resolution, respectively. Two good heavy atom derivatives were, found and used for multiple isomorphous replacement phasing. The atomic, coordinates were refined using the Hendrickson &amp; Konnert program for, stereochemically restrained refinement against structure factors. The, crystallographic R factors were reduced to 15.3% for the serine analogue, structure and 16.0% for the wild-type structure. The serine analogue and, wild-type structures have been found to be almost identical, the, root-mean-square deviation between the corresponding C alpha atoms being, 0.11 A. Their structures are composed of twelve beta-strands forming a, barrel and three loops. Their molecules have an approximate threefold, internal symmetry and are similar in architecture to that of interleukin-1, beta. A possible heparin-binding site, which comprises five basic, residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by, calculating the electrostatic potential energy.
+We have determined the crystal structures of two types of human basic fibroblast growth factor, the serine analogue and the wild-type, at 1.6 and 2.5 A resolution, respectively. Two good heavy atom derivatives were found and used for multiple isomorphous replacement phasing. The atomic coordinates were refined using the Hendrickson &amp; Konnert program for stereochemically restrained refinement against structure factors. The crystallographic R factors were reduced to 15.3% for the serine analogue structure and 16.0% for the wild-type structure. The serine analogue and wild-type structures have been found to be almost identical, the root-mean-square deviation between the corresponding C alpha atoms being 0.11 A. Their structures are composed of twelve beta-strands forming a barrel and three loops. Their molecules have an approximate threefold internal symmetry and are similar in architecture to that of interleukin-1 beta. A possible heparin-binding site, which comprises five basic residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by calculating the electrostatic potential energy.
 ==Disease==
@@ Line 13: / Line 13: @@
 ==Reference==
-Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem (Tokyo). 1991 Sep;110(3):360-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1769963 1769963]
+Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem. 1991 Sep;110(3):360-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1769963 1769963]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
@@ Line 23: / Line 23: @@
 [[Category: growth factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:16:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:15 2008''