This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Insulin receptor

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
'''Insulin receptor''' (IR) is a transmembrane receptor activated by insulin, IGF-I and IGF-II. IR is important for the regulation of glucose homeostasis and its malfunction can cause diabetics and cancer. The IR is a dimer where each monomer contains 8 distinct domains. The β-chain contains a tyrosine kinase catalytic domain (TK).<br />
'''Insulin receptor''' (IR) is a transmembrane receptor activated by insulin, IGF-I and IGF-II. IR is important for the regulation of glucose homeostasis and its malfunction can cause diabetics and cancer. The IR is a dimer where each monomer contains 8 distinct domains. The β-chain contains a tyrosine kinase catalytic domain (TK).<br />
-
See also [[Insulin Receptor kinase domain (hebrew)]].
+
See also [[Insulin Receptor - kinase domain (hebrew)]].
==3D structures of insulin receptor==
==3D structures of insulin receptor==

Revision as of 12:44, 6 January 2016

Structure of human insulin receptor tyrosine kinase catalytic domain complex with insulin receptor substrate 2 peptide (green), Mg+2 ion (green) and ATP (stick model) (PDB entry 3bu5)

Drag the structure with the mouse to rotate
Personal tools