3bvg

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[[Image:3bvg.png|left|200px]]
[[Image:3bvg.png|left|200px]]
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{{STRUCTURE_3bvg| PDB=3bvg | SCENE= }}
{{STRUCTURE_3bvg| PDB=3bvg | SCENE= }}
===Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex===
===Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex===
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{{ABSTRACT_PUBMED_20836565}}
{{ABSTRACT_PUBMED_20836565}}
==About this Structure==
==About this Structure==
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3BVG is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BVG OCA].
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[[3bvg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BVG OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:20836565</ref><references group="xtra"/>
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<ref group="xtra">PMID:020836565</ref><references group="xtra"/>
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Cho, S.]]
[[Category: Cho, S.]]
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[[Category: Superantigen]]
[[Category: Superantigen]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 10 06:54:26 2010''
 

Revision as of 20:30, 7 January 2013

Template:STRUCTURE 3bvg

Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex

Template:ABSTRACT PUBMED 20836565

About this Structure

3bvg is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

  • Cho S, Swaminathan CP, Bonsor DA, Kerzic MC, Guan R, Yang J, Kieke MC, Andersen PS, Kranz DM, Mariuzza RA, Sundberg EJ. Assessing energetic contributions to binding from a disordered region in a protein-protein interaction . Biochemistry. 2010 Nov 2;49(43):9256-68. PMID:20836565 doi:10.1021/bi1008968

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