1hyj: Difference between revisions

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==Overview==

The recruitment of trafficking and signaling proteins to membranes, containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by, FYVE domains. Here, the solution structure of the FYVE domain of the early, endosome antigen 1 protein (EEA1) in the free state was compared with the, structures of the domain complexed with PtdIns(3)P and mixed micelles. The, multistep binding mechanism involved nonspecific insertion of a, hydrophobic loop into the lipid bilayer, positioning and activating the, binding pocket. Ligation of PtdIns(3)P then induced a global structural, change, drawing the protein termini over the bound phosphoinositide by, extension of a hinge. Specific recognition of the 3-phosphate was, determined indirectly and directly by two clusters of conserved arginines.

The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.

==Disease==

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[[Category: zinc cluster]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:05 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The recruitment of trafficking and signaling proteins to membranes, containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by, FYVE domains. Here, the solution structure of the FYVE domain of the early, endosome antigen 1 protein (EEA1) in the free state was compared with the, structures of the domain complexed with PtdIns(3)P and mixed micelles. The, multistep binding mechanism involved nonspecific insertion of a, hydrophobic loop into the lipid bilayer, positioning and activating the, binding pocket. Ligation of PtdIns(3)P then induced a global structural, change, drawing the protein termini over the bound phosphoinositide by, extension of a hinge. Specific recognition of the 3-phosphate was, determined indirectly and directly by two clusters of conserved arginines.
+The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.
 ==Disease==
@@ Line 23: / Line 23: @@
 [[Category: zinc cluster]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:58:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:05 2008''