2gzh: Difference between revisions

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==Overview==

The small GTPase Rab11 regulates the recycling of endosomes to the plasma, membrane via interactions with the Rab11 family of interacting proteins, (FIPs). FIPs contain a highly conserved Rab binding domain (RBD) at their, C termini whose structure is unknown. Here, we have determined the crystal, structure of the RBD of FIP2 in complex with Rab11(GTP) by single, wavelength anomalous diffraction methods. The overall structure is a, heterotetramer with dyad symmetry, arranged as a Rab11-(FIP2)2-Rab11, complex. FIP2 forms a central alpha-helical coiled coil, with both helices, contributing to the Rab11 binding patch on equivalent and opposite sides, of the homodimer. Switch 1 of Rab11 is embedded between the two helices, while switch 2 remains flexible and is peripherally associated with the, effector. The complex reveals the structural basis for Rab11 recognition, by FIPs and suggests the molecular mechanisms underlying endocytic, recycling pathways.

The small GTPase Rab11 regulates the recycling of endosomes to the plasma membrane via interactions with the Rab11 family of interacting proteins (FIPs). FIPs contain a highly conserved Rab binding domain (RBD) at their C termini whose structure is unknown. Here, we have determined the crystal structure of the RBD of FIP2 in complex with Rab11(GTP) by single wavelength anomalous diffraction methods. The overall structure is a heterotetramer with dyad symmetry, arranged as a Rab11-(FIP2)2-Rab11 complex. FIP2 forms a central alpha-helical coiled coil, with both helices contributing to the Rab11 binding patch on equivalent and opposite sides of the homodimer. Switch 1 of Rab11 is embedded between the two helices, while switch 2 remains flexible and is peripherally associated with the effector. The complex reveals the structural basis for Rab11 recognition by FIPs and suggests the molecular mechanisms underlying endocytic recycling pathways.

==About this Structure==

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[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Khan, A.R.]]

[[Category: Khan, A R.]]

[[Category: GTP]]

[[Category: MG]]

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[[Category: ras-like g protein fold]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:37 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The small GTPase Rab11 regulates the recycling of endosomes to the plasma, membrane via interactions with the Rab11 family of interacting proteins, (FIPs). FIPs contain a highly conserved Rab binding domain (RBD) at their, C termini whose structure is unknown. Here, we have determined the crystal, structure of the RBD of FIP2 in complex with Rab11(GTP) by single, wavelength anomalous diffraction methods. The overall structure is a, heterotetramer with dyad symmetry, arranged as a Rab11-(FIP2)2-Rab11, complex. FIP2 forms a central alpha-helical coiled coil, with both helices, contributing to the Rab11 binding patch on equivalent and opposite sides, of the homodimer. Switch 1 of Rab11 is embedded between the two helices, while switch 2 remains flexible and is peripherally associated with the, effector. The complex reveals the structural basis for Rab11 recognition, by FIPs and suggests the molecular mechanisms underlying endocytic, recycling pathways.
+The small GTPase Rab11 regulates the recycling of endosomes to the plasma membrane via interactions with the Rab11 family of interacting proteins (FIPs). FIPs contain a highly conserved Rab binding domain (RBD) at their C termini whose structure is unknown. Here, we have determined the crystal structure of the RBD of FIP2 in complex with Rab11(GTP) by single wavelength anomalous diffraction methods. The overall structure is a heterotetramer with dyad symmetry, arranged as a Rab11-(FIP2)2-Rab11 complex. FIP2 forms a central alpha-helical coiled coil, with both helices contributing to the Rab11 binding patch on equivalent and opposite sides of the homodimer. Switch 1 of Rab11 is embedded between the two helices, while switch 2 remains flexible and is peripherally associated with the effector. The complex reveals the structural basis for Rab11 recognition by FIPs and suggests the molecular mechanisms underlying endocytic recycling pathways.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Khan, A.R.]]
+[[Category: Khan, A R.]]
 [[Category: GTP]]
 [[Category: MG]]
@@ Line 20: / Line 20: @@
 [[Category: ras-like g protein fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:29:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:37 2008''