2kin
From Proteopedia
(New page: 200px<br /> <applet load="2kin" size="450" color="white" frame="true" align="right" spinBox="true" caption="2kin, resolution 2.Å" /> '''KINESIN (MONOMERIC) F...) |
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| - | [[Image:2kin.gif|left|200px]]<br /> | + | [[Image:2kin.gif|left|200px]]<br /><applet load="2kin" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2kin" size=" | + | |
caption="2kin, resolution 2.Å" /> | caption="2kin, resolution 2.Å" /> | ||
'''KINESIN (MONOMERIC) FROM RATTUS NORVEGICUS'''<br /> | '''KINESIN (MONOMERIC) FROM RATTUS NORVEGICUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the X-ray structure of rat kinesin head and neck | + | We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550-554]. Novel features of the structure include the N-terminal region, folded as a beta-strand, and the C-terminal transition from the motor to the rod domain, folded as two beta-strands plus an alpha-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959-966], take the form of beta-strands attached to the central beta-sheet of the structure. |
==About this Structure== | ==About this Structure== | ||
| - | 2KIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2KIN with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb64_1.html Kinesin]]. Full crystallographic information is available from [http:// | + | 2KIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2KIN with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb64_1.html Kinesin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Biou, V.]] | [[Category: Biou, V.]] | ||
| - | [[Category: Brady, S | + | [[Category: Brady, S T.]] |
[[Category: Kozielski, F.]] | [[Category: Kozielski, F.]] | ||
[[Category: Mandelkow, E.]] | [[Category: Mandelkow, E.]] | ||
| - | [[Category: Mandelkow, E | + | [[Category: Mandelkow, E M.]] |
[[Category: Marx, A.]] | [[Category: Marx, A.]] | ||
[[Category: Muller, J.]] | [[Category: Muller, J.]] | ||
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[[Category: motor protein]] | [[Category: motor protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:53 2008'' |
Revision as of 16:06, 21 February 2008
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KINESIN (MONOMERIC) FROM RATTUS NORVEGICUS
Overview
We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550-554]. Novel features of the structure include the N-terminal region, folded as a beta-strand, and the C-terminal transition from the motor to the rod domain, folded as two beta-strands plus an alpha-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959-966], take the form of beta-strands attached to the central beta-sheet of the structure.
About this Structure
2KIN is a Protein complex structure of sequences from Rattus norvegicus with and as ligands. The following page contains interesting information on the relation of 2KIN with [Kinesin]. Full crystallographic information is available from OCA.
Reference
X-ray structure of motor and neck domains from rat brain kinesin., Sack S, Muller J, Marx A, Thormahlen M, Mandelkow EM, Brady ST, Mandelkow E, Biochemistry. 1997 Dec 23;36(51):16155-65. PMID:9405049
Page seeded by OCA on Thu Feb 21 18:06:53 2008
Categories: Kinesin | Protein complex | Rattus norvegicus | Biou, V. | Brady, S T. | Kozielski, F. | Mandelkow, E. | Mandelkow, E M. | Marx, A. | Muller, J. | Sack, S. | Thormahlen, M. | ADP | SO4 | Cytoskeleton | Motor protein
