This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1sz4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1sz4" [edit=sysop:move=sysop])
Line 1: Line 1:
-
{{Theoretical_model}}
+
==MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE 2'-SLADP BOUND AT THE NUCLEOTIDE SITE==
 +
<StructureSection load='1sz4' size='340' side='right' caption='[[1sz4]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SZ4 FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sz4 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1sz4 PDBsum]</span></td></tr>
 +
<table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
[[Image:1sz4.png|left|200px]]
+
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>
-
{{STRUCTURE_1sz4| PDB=1sz4 | SCENE= }}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
===MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE 2'-SLADP BOUND AT THE NUCLEOTIDE SITE===
+
== References ==
-
 
+
<references/>
-
{{ABSTRACT_PUBMED_12730601}}
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
<ref group="xtra">PMID:012730601</ref><references group="xtra"/>
+
[[Category: Car, R]]
[[Category: Car, R]]
[[Category: Chen, X]]
[[Category: Chen, X]]

Revision as of 22:05, 28 September 2014

MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE 2'-SLADP BOUND AT THE NUCLEOTIDE SITE

1sz4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sz4"
Views
Personal tools
Navigation
Toolbox