2v14
From Proteopedia
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==Overview== | ==Overview== | ||
| - | KIF16B is a newly identified kinesin that regulates the intracellular | + | KIF16B is a newly identified kinesin that regulates the intracellular motility of early endosomes. KIF16B is unique among kinesins in that its cargo binding is mediated primarily by the strong interaction of its PX domain with endosomal lipids. To elucidate the structural basis of this unique endosomal anchoring activity of KIF16B-PX, we determined the crystal structure of the PX domain and performed in vitro and cellular membrane binding measurements for KIF16B-PX and mutants. The most salient structural feature of KIF16B-PX is that two neighboring residues, L1248 and F1249, on the membrane-binding surface form a protruding hydrophobic stalk with a large solvent-accessible surface area. This unique structure, arising from the complementary stacking of the two side chains and the local conformation, allows strong hydrophobic membrane interactions and endosome tethering. The presence of similar hydrophobic pairs in the amino-acid sequences of other membrane-binding domains and proteins suggests that the same structural motif may be shared by other membrane-binding proteins, whose physiological functions depend on strong hydrophobic membrane interactions. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | The structural basis of novel endosome anchoring activity of KIF16B kinesin., Blatner NR, Wilson MI, Lei C, Hong W, Murray D, Williams RL, Cho W, EMBO J. 2007 Jul 19 | + | The structural basis of novel endosome anchoring activity of KIF16B kinesin., Blatner NR, Wilson MI, Lei C, Hong W, Murray D, Williams RL, Cho W, EMBO J. 2007 Aug 8;26(15):3709-19. Epub 2007 Jul 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17641687 17641687] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blatner, N | + | [[Category: Blatner, N R.]] |
[[Category: Cho, W.]] | [[Category: Cho, W.]] | ||
[[Category: Hong, W.]] | [[Category: Hong, W.]] | ||
| - | [[Category: Williams, R | + | [[Category: Williams, R L.]] |
| - | [[Category: Wilson, M | + | [[Category: Wilson, M I.]] |
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
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[[Category: ubl conjugation]] | [[Category: ubl conjugation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:52:27 2008'' |
Revision as of 16:52, 21 February 2008
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KINESIN 16B PHOX-HOMOLOGY DOMAIN (KIF16B)
Overview
KIF16B is a newly identified kinesin that regulates the intracellular motility of early endosomes. KIF16B is unique among kinesins in that its cargo binding is mediated primarily by the strong interaction of its PX domain with endosomal lipids. To elucidate the structural basis of this unique endosomal anchoring activity of KIF16B-PX, we determined the crystal structure of the PX domain and performed in vitro and cellular membrane binding measurements for KIF16B-PX and mutants. The most salient structural feature of KIF16B-PX is that two neighboring residues, L1248 and F1249, on the membrane-binding surface form a protruding hydrophobic stalk with a large solvent-accessible surface area. This unique structure, arising from the complementary stacking of the two side chains and the local conformation, allows strong hydrophobic membrane interactions and endosome tethering. The presence of similar hydrophobic pairs in the amino-acid sequences of other membrane-binding domains and proteins suggests that the same structural motif may be shared by other membrane-binding proteins, whose physiological functions depend on strong hydrophobic membrane interactions.
About this Structure
2V14 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structural basis of novel endosome anchoring activity of KIF16B kinesin., Blatner NR, Wilson MI, Lei C, Hong W, Murray D, Williams RL, Cho W, EMBO J. 2007 Aug 8;26(15):3709-19. Epub 2007 Jul 19. PMID:17641687
Page seeded by OCA on Thu Feb 21 18:52:27 2008
Categories: Homo sapiens | Single protein | Blatner, N R. | Cho, W. | Hong, W. | Williams, R L. | Wilson, M I. | Alternative splicing | Atp-binding | Coiled coil | Endosome transport | Microtubule | Motor protein | Nucleotide-binding | Phosphatidylinositol 3-phosphate binding | Plus-end kinesin complex | Plus-end-directed microtubule motor activity | Polymorphism | Transport protein | Ubl conjugation
