1t5c

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|PDB= 1t5c |SIZE=350|CAPTION= <scene name='initialview01'>1t5c</scene>, resolution 2.5&Aring;
|PDB= 1t5c |SIZE=350|CAPTION= <scene name='initialview01'>1t5c</scene>, resolution 2.5&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=PIN:PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID)'>PIN</scene>
+
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=PIN:PIPERAZINE-N,N&#39;-BIS(2-ETHANESULFONIC ACID)'>PIN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= CENPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= CENPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:14:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:41:42 2008''

Revision as of 11:41, 23 March 2008

Image:1t5c.gif


PDB ID 1t5c

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , , and
Gene: CENPE (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the motor domain of human kinetochore protein CENP-E


Overview

The human kinetochore is a highly complex macromolecular structure that connects chromosomes to spindle microtubules (MTs) in order to facilitate accurate chromosome segregation. Centromere-associated protein E (CENP-E), a member of the kinesin superfamily, is an essential component of the kinetochore, since it is required to stabilize the attachment of chromosomes to spindle MTs, to develop tension across aligned chromosomes, to stabilize spindle poles and to satisfy the mitotic checkpoint. Here we report the 2.5A resolution crystal structure of the motor domain and linker region of human CENP-E with MgADP bound in the active site. This structure displays subtle but important differences compared to the structures of human Eg5 and conventional kinesin. Our structure reveals that the CENP-E linker region is in a "docked" position identical to that in the human plus-end directed conventional kinesin. CENP-E has many advantages as a potential anti-mitotic drug target and this crystal structure of human CENP-E will provide a starting point for high throughput virtual screening of potential inhibitors.

About this Structure

1T5C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the motor domain of the human kinetochore protein CENP-E., Garcia-Saez I, Yen T, Wade RH, Kozielski F, J Mol Biol. 2004 Jul 23;340(5):1107-16. PMID:15236970

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