1jl9: Difference between revisions

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==Overview==

Epidermal growth factor (EGF) is a typical growth-stimulating peptide and, functions by binding to specific cell-surface receptors and inducing, dimerization of the receptors. Little is known about the molecular, mechanism of EGF-induced dimerization of EGF receptors. The crystal, structure of human EGF has been determined at pH 8.1. There are two human, EGF molecules A and B in the asymmetric unit of the crystals, which form a, potential dimer. Importantly, a number of residues known to be, indispensable for EGF binding to its receptor are involved in the, interface between the two EGF molecules, suggesting a crucial role of EGF, dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure, of mouse EGF determined at pH 2.0, but structural comparisons between, different models have revealed new detailed features and properties of the, EGF structure.

Epidermal growth factor (EGF) is a typical growth-stimulating peptide and functions by binding to specific cell-surface receptors and inducing dimerization of the receptors. Little is known about the molecular mechanism of EGF-induced dimerization of EGF receptors. The crystal structure of human EGF has been determined at pH 8.1. There are two human EGF molecules A and B in the asymmetric unit of the crystals, which form a potential dimer. Importantly, a number of residues known to be indispensable for EGF binding to its receptor are involved in the interface between the two EGF molecules, suggesting a crucial role of EGF dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure of mouse EGF determined at pH 2.0, but structural comparisons between different models have revealed new detailed features and properties of the EGF structure.

==Disease==

Known disease associated with this structure: Hypomagnesemia 4, renal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131530 131530]]

==About this Structure==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Bi, R.C.]]

[[Category: Bi, R C.]]

[[Category: Chai, J.J.]]

[[Category: Chai, J J.]]

[[Category: He, C.H.]]

[[Category: He, C H.]]

[[Category: Huang, B.R.]]

[[Category: Huang, B R.]]

[[Category: Li, M.]]

[[Category: Lu, H.S.]]

[[Category: Lu, H S.]]

[[Category: dimerization]]

[[Category: growth factor]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Epidermal growth factor (EGF) is a typical growth-stimulating peptide and, functions by binding to specific cell-surface receptors and inducing, dimerization of the receptors. Little is known about the molecular, mechanism of EGF-induced dimerization of EGF receptors. The crystal, structure of human EGF has been determined at pH 8.1. There are two human, EGF molecules A and B in the asymmetric unit of the crystals, which form a, potential dimer. Importantly, a number of residues known to be, indispensable for EGF binding to its receptor are involved in the, interface between the two EGF molecules, suggesting a crucial role of EGF, dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure, of mouse EGF determined at pH 2.0, but structural comparisons between, different models have revealed new detailed features and properties of the, EGF structure.
+Epidermal growth factor (EGF) is a typical growth-stimulating peptide and functions by binding to specific cell-surface receptors and inducing dimerization of the receptors. Little is known about the molecular mechanism of EGF-induced dimerization of EGF receptors. The crystal structure of human EGF has been determined at pH 8.1. There are two human EGF molecules A and B in the asymmetric unit of the crystals, which form a potential dimer. Importantly, a number of residues known to be indispensable for EGF binding to its receptor are involved in the interface between the two EGF molecules, suggesting a crucial role of EGF dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure of mouse EGF determined at pH 2.0, but structural comparisons between different models have revealed new detailed features and properties of the EGF structure.
+==Disease==
+Known disease associated with this structure: Hypomagnesemia 4, renal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131530 131530]]
 ==About this Structure==
@@ Line 13: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Bi, R.C.]]
+[[Category: Bi, R C.]]
-[[Category: Chai, J.J.]]
+[[Category: Chai, J J.]]
-[[Category: He, C.H.]]
+[[Category: He, C H.]]
-[[Category: Huang, B.R.]]
+[[Category: Huang, B R.]]
 [[Category: Li, M.]]
-[[Category: Lu, H.S.]]
+[[Category: Lu, H S.]]
 [[Category: dimerization]]
 [[Category: growth factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:42:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:55 2008''