2la1

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[[Image:2la1.png|left|200px]]
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==Expression in Pichia pastoris and backbone dynamics of dendroaspin, a three finger toxin==
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<StructureSection load='2la1' size='340' side='right' caption='[[2la1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2la1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dendroaspis_jamesoni_kaimosae Dendroaspis jamesoni kaimosae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LA1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LA1 FirstGlance]. <br>
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</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=2la1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2la1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2la1 RCSB], [http://www.ebi.ac.uk/pdbsum/2la1 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dendroaspin (Den) and rhodostomin (Rho) are snake venom proteins containing a PRGDMP motif. Although Den and Rho have different 3D structures, they are highly potent integrin inhibitors. To study their structure, function, and dynamics relationships, we expressed Den and Rho in Pichia pastoris. The recombinant Den and Rho inhibited platelet aggregation with the K(I) values of 149.8 and 83.2 nM. Cell adhesion analysis showed that Den was 3.7 times less active than Rho when inhibiting the integrin alphaIIbbeta3 and 2.5 times less active when inhibiting the integrin alphavbeta3. In contrast, Den and Rho were similarly active when inhibiting the integrin alpha5beta1 with the IC(50) values of 239.8 and 256.8 nM. NMR analysis showed that recombinant Den and Rho have different 3D conformations for their arginyl-glycyl-aspartic acid (RGD) motif. However, the comparison with Rho showed that the docking of Den into integrin alphavbeta3 resulted in a similar number of contacts. Analysis of the dynamic properties of the RGD loop in Den and Rho showed that they also had different dynamic properties. These results demonstrate that protein scaffolds affect the function, structure, and dynamics of their RGD motif.
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{{STRUCTURE_2la1| PDB=2la1 | SCENE= }}
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Dynamics and functional differences between dendroaspin and rhodostomin: Insights into protein scaffolds in integrin recognition.,Cheng CH, Chen YC, Shiu JH, Chang YT, Chang YS, Huang CH, Chen CY, Chuang WJ Protein Sci. 2012 Dec;21(12):1872-84. doi: 10.1002/pro.2169. Epub 2012 Nov 6. PMID:23033223<ref>PMID:23033223</ref>
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===Expression in Pichia pastoris and backbone dynamics of dendroaspin, a three finger toxin===
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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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{{ABSTRACT_PUBMED_23033223}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2la1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dendroaspis_jamesoni_kaimosae Dendroaspis jamesoni kaimosae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LA1 OCA].
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</StructureSection>
[[Category: Dendroaspis jamesoni kaimosae]]
[[Category: Dendroaspis jamesoni kaimosae]]
[[Category: Chen, Y C.]]
[[Category: Chen, Y C.]]

Revision as of 00:54, 2 October 2014

Expression in Pichia pastoris and backbone dynamics of dendroaspin, a three finger toxin

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