1l2n: Difference between revisions
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==Smt3 Solution Structure== | ==Smt3 Solution Structure== | ||
<StructureSection load='1l2n' size='340' side='right' caption='[[1l2n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1l2n' size='340' side='right'caption='[[1l2n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1l2n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L2N FirstGlance]. <br> | <table><tr><td colspan='2'>[[1l2n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L2N FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1l2n" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1l2n" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[SUMO|SUMO]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | |||
[[Category: Liao, X]] | [[Category: Liao, X]] | ||
[[Category: Sheng, W]] | [[Category: Sheng, W]] |
Revision as of 15:00, 13 November 2019
Smt3 Solution StructureSmt3 Solution Structure
Structural highlights
Function[SMT3_YEAST] Not known; suppressor of MIF2 mutations. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSmt3 belongs to a growing family of ubiquitin-related proteins involved in posttranslational protein modification. Independent studies demonstrate an essential function of Smt3 in the regulation of nucleocytoplasmic transport, and suggest a role in cell-cycle regulation. Here we report the high-resolution NMR structure of yeast Smt3 in the complex free form. Our comparison of the Smt3 NMR structure with the Smt3 crystal structure in complex with the C-Terminal Ulp1 protease domain revealed large structural differences in the binding surface, which is also involved in the Smt3-Ubc-9 interaction detected by NMR. The structural differences in the region indicate the important functions of conserved residues in less structurally defined sequences. Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions.,Sheng W, Liao X Protein Sci. 2002 Jun;11(6):1482-91. PMID:12021447[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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