3kin

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|PDB= 3kin |SIZE=350|CAPTION= <scene name='initialview01'>3kin</scene>, resolution 3.1&Aring;
|PDB= 3kin |SIZE=350|CAPTION= <scene name='initialview01'>3kin</scene>, resolution 3.1&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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[[Category: motor protein]]
[[Category: motor protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:05:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 16:02:46 2008''

Revision as of 14:02, 23 March 2008

Image:3kin.gif


PDB ID 3kin

Drag the structure with the mouse to rotate
, resolution 3.1Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



KINESIN (DIMERIC) FROM RATTUS NORVEGICUS


Overview

The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are connected via a coiled-coil alpha-helical interaction of their necks. They are broadly similar to one another; differences are most apparent in the head-neck junction and in a moderate reorientation of the neck helices in order to adopt to the coiled-coil conformation. The heads show a rotational symmetry (approximately 120 degrees) about an axis close to that of the coiled-coil. This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules.

About this Structure

3KIN is a Protein complex structure of sequences from Rattus norvegicus. The following page contains interesting information on the relation of 3KIN with [Kinesin]. Full crystallographic information is available from OCA.

Reference

The crystal structure of dimeric kinesin and implications for microtubule-dependent motility., Kozielski F, Sack S, Marx A, Thormahlen M, Schonbrunn E, Biou V, Thompson A, Mandelkow EM, Mandelkow E, Cell. 1997 Dec 26;91(7):985-94. PMID:9428521

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