3ux3
From Proteopedia
(Difference between revisions)
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==Crystal Structure of Domain-Swapped Fam96a minor dimer== | ==Crystal Structure of Domain-Swapped Fam96a minor dimer== | ||
| - | <StructureSection load='3ux3' size='340' side='right' caption='[[3ux3]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3ux3' size='340' side='right'caption='[[3ux3]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ux3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UX3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3ux3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UX3 FirstGlance]. <br> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FA96A_HUMAN FA96A_HUMAN]] May play a role in chromosome segregation through establishment of sister chromatid cohesion (By similarity). | [[http://www.uniprot.org/uniprot/FA96A_HUMAN FA96A_HUMAN]] May play a role in chromosome segregation through establishment of sister chromatid cohesion (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fam96a mRNA, which encodes a mammalian DUF59 protein, is enriched in macrophages. Recombinant human Fam96a forms stable monomers and dimers in solution. Crystal structures of these two forms revealed that each adopts a distinct type of domain-swapped dimer, one of which is stabilized by zinc binding. Two hinge loops control Fam96a domain swapping; both are flexible and highly conserved, suggesting that domain swapping may be a common feature of eukaryotic but not bacterial DUF59 proteins. The derived monomer fold of Fam96a diverges from that of bacterial DUF59 counterparts in that the C-terminal region of Fam96a is much longer and is positioned on the opposite side of the N-terminal core fold. The putative metal-binding site of bacterial DUF59 proteins is not conserved in Fam96a, but Fam96a interacts tightly in vitro with Ciao1, the cytosolic iron-assembly protein. Moreover, Fam96a and Ciao1 can be co-immunoprecipitated, suggesting that the interaction also occurs in vivo. Although predicted to have a signal peptide, it is shown that Fam96a is cytoplasmic. The data reveal that eukaryotic DUF59 proteins share intriguing characteristics with amyloidogenic proteins. | ||
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| + | The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer.,Chen KE, Richards AA, Ariffin JK, Ross IL, Sweet MJ, Kellie S, Kobe B, Martin JL Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):637-48. doi:, 10.1107/S0907444912006592. Epub 2012 May 17. PMID:22683786<ref>PMID:22683786</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3ux3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Chen, K E]] | [[Category: Chen, K E]] | ||
[[Category: Kobe, B]] | [[Category: Kobe, B]] | ||
Revision as of 08:35, 1 January 2020
Crystal Structure of Domain-Swapped Fam96a minor dimer
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