1m6b: Difference between revisions

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==Overview==

We have determined the 2.6 angstrom crystal structure of the entire, extracellular region of human HER3 (ErbB3), a member of the epidermal, growth factor receptor (EGFR) family. The structure consists of four, domains with structural homology to domains found in the type I, insulin-like growth factor receptor. The HER3 structure reveals a contact, between domains II and IV that constrains the relative orientations of, ligand-binding domains and provides a structural basis for understanding, both multiple-affinity forms of EGFRs and conformational changes induced, in the receptor by ligand binding during signaling. These results also, suggest new therapeutic approaches to modulating the behavior of members, of the EGFR family.

We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family. The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor. The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling. These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.

==Disease==

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[[Category: Single protein]]

[[Category: Transferase]]

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

[[Category: Cho, H S.]]

[[Category: Leahy, D.J.]]

[[Category: Leahy, D J.]]

[[Category: NAG]]

[[Category: NDG]]

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[[Category: tyrosine kinase; cell surface receptor; immunity]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:58 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-We have determined the 2.6 angstrom crystal structure of the entire, extracellular region of human HER3 (ErbB3), a member of the epidermal, growth factor receptor (EGFR) family. The structure consists of four, domains with structural homology to domains found in the type I, insulin-like growth factor receptor. The HER3 structure reveals a contact, between domains II and IV that constrains the relative orientations of, ligand-binding domains and provides a structural basis for understanding, both multiple-affinity forms of EGFRs and conformational changes induced, in the receptor by ligand binding during signaling. These results also, suggest new therapeutic approaches to modulating the behavior of members, of the EGFR family.
+We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family. The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor. The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling. These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Transferase]]
-[[Category: Cho, H.S.]]
+[[Category: Cho, H S.]]
-[[Category: Leahy, D.J.]]
+[[Category: Leahy, D J.]]
 [[Category: NAG]]
 [[Category: NDG]]
@@ Line 24: / Line 24: @@
 [[Category: tyrosine kinase; cell surface receptor; immunity]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:22:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:58 2008''