1t5c: Difference between revisions

Revision as of 01:01, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1t5c.png

Template:STRUCTURE 1t5c

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

Template:ABSTRACT PUBMED 15236970

About this StructureAbout this Structure

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

ReferenceReference

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

Crystallization and preliminary crystallographic analysis of the motor domain of human kinetochore-associated protein CENP-E using an automated crystallization procedure., Garcia-Saez I, Blot D, Kahn R, Kozielski F, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1158-60. Epub 2004, May 21. PMID:15159587

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OCA

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-'''Crystal structure of the motor domain of human kinetochore protein CENP-E'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15236970}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15236970 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15236970}}
 ==About this Structure==
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 ==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:[http://www.ncbi.nlm.nih.gov/pubmed/15236970 15236970]
+Crystallization and preliminary crystallographic analysis of the motor domain of human kinetochore-associated protein CENP-E using an automated crystallization procedure., Garcia-Saez I, Blot D, Kahn R, Kozielski F, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1158-60. Epub 2004, May 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15159587 15159587]
 [[Category: Homo sapiens]]
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 [[Category: Structural genomic]]
 [[Category: Structural proteomics in europe]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:11:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:01:21 2008''