1syp

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1syp.png|left|200px]]
 
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==MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE SL-NANDP BOUND AT THE NUCLEOTIDE SITE==
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The line below this paragraph, containing "STRUCTURE_1syp", creates the "Structure Box" on the page.
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<StructureSection load='1syp' size='340' side='right'caption='[[1syp]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYP FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1syp FirstGlance], [https://www.ebi.ac.uk/pdbsum/1syp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1syp ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1syp| PDB=1syp | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have used adenosine diphosphate analogs containing electron paramagnetic resonance (EPR) spin moieties and EPR spectroscopy to show that the nucleotide-binding site of kinesin-family motors closes when the motor.diphosphate complex binds to microtubules. Structural analyses demonstrate that a domain movement in the switch 1 region at the nucleotide site, homologous to domain movements in the switch 1 region in the G proteins [heterotrimeric guanine nucleotide-binding proteins], explains the EPR data. The switch movement primes the motor both for the free energy-yielding nucleotide hydrolysis reaction and for subsequent conformational changes that are crucial for the generation of force and directed motion along the microtubule.
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===MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE SL-NANDP BOUND AT THE NUCLEOTIDE SITE===
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Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules.,Naber N, Minehardt TJ, Rice S, Chen X, Grammer J, Matuska M, Vale RD, Kollman PA, Car R, Yount RG, Cooke R, Pate E Science. 2003 May 2;300(5620):798-801. PMID:12730601<ref>PMID:12730601</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12730601}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1syp" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12730601 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12730601}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYP OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:12730601</ref><references group="xtra"/>
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[[Category: Car, R]]
[[Category: Car, R]]
[[Category: Chen, X]]
[[Category: Chen, X]]
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[[Category: Vale, R D]]
[[Category: Vale, R D]]
[[Category: Yount, R G]]
[[Category: Yount, R G]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 09:10:17 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE SL-NANDP BOUND AT THE NUCLEOTIDE SITE

PDB ID 1syp

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