1cvs: Difference between revisions

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==Overview==

The crystal structure of FGF2 bound to a naturally occurring variant of, FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2), and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1, complexes form a 2-fold symmetric dimer. Within each complex, FGF2, interacts extensively with D2 and D3 as well as with the linker between, the two domains. The dimer is stabilized by interactions between FGF2 and, D2 of the adjoining complex and by a direct interaction between D2 of each, receptor. A positively charged canyon formed by a cluster of exposed basic, residues likely represents the heparin-binding site. A general model for, FGF- and heparin-induced FGFR dimerization is inferred from the crystal, structure, unifying a wealth of biochemical data.

The crystal structure of FGF2 bound to a naturally occurring variant of FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2) and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1 complexes form a 2-fold symmetric dimer. Within each complex, FGF2 interacts extensively with D2 and D3 as well as with the linker between the two domains. The dimer is stabilized by interactions between FGF2 and D2 of the adjoining complex and by a direct interaction between D2 of each receptor. A positively charged canyon formed by a cluster of exposed basic residues likely represents the heparin-binding site. A general model for FGF- and heparin-induced FGFR dimerization is inferred from the crystal structure, unifying a wealth of biochemical data.

==Disease==

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[[Category: Homo sapiens]]

[[Category: Protein complex]]

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

[[Category: Hubbard, S R.]]

[[Category: Mohammadi, M.]]

[[Category: Plotnikov, A.N.]]

[[Category: Plotnikov, A N.]]

[[Category: Schlessinger, J.]]

[[Category: SO4]]

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[[Category: signal transduction]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structure of FGF2 bound to a naturally occurring variant of, FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2), and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1, complexes form a 2-fold symmetric dimer. Within each complex, FGF2, interacts extensively with D2 and D3 as well as with the linker between, the two domains. The dimer is stabilized by interactions between FGF2 and, D2 of the adjoining complex and by a direct interaction between D2 of each, receptor. A positively charged canyon formed by a cluster of exposed basic, residues likely represents the heparin-binding site. A general model for, FGF- and heparin-induced FGFR dimerization is inferred from the crystal, structure, unifying a wealth of biochemical data.
+The crystal structure of FGF2 bound to a naturally occurring variant of FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2) and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1 complexes form a 2-fold symmetric dimer. Within each complex, FGF2 interacts extensively with D2 and D3 as well as with the linker between the two domains. The dimer is stabilized by interactions between FGF2 and D2 of the adjoining complex and by a direct interaction between D2 of each receptor. A positively charged canyon formed by a cluster of exposed basic residues likely represents the heparin-binding site. A general model for FGF- and heparin-induced FGFR dimerization is inferred from the crystal structure, unifying a wealth of biochemical data.
 ==Disease==
@@ Line 16: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Hubbard, S.R.]]
+[[Category: Hubbard, S R.]]
 [[Category: Mohammadi, M.]]
-[[Category: Plotnikov, A.N.]]
+[[Category: Plotnikov, A N.]]
 [[Category: Schlessinger, J.]]
 [[Category: SO4]]
@@ Line 27: / Line 27: @@
 [[Category: signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:37:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:14 2008''