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2ROT

Structure of chimeric variant of SH3 domain- SHH

Summary for 2ROT
Entry DOI10.2210/pdb2rot/pdb
NMR InformationBMRB: 11043
DescriptorSpectrin alpha chain, brain (1 entity in total)
Functional Keywordssh3, chimeric protein, alpha-spectrin, actin capping, actin-binding, calcium, calmodulin-binding, cytoplasm, cytoskeleton, phosphoprotein, sh3 domain, protein binding
Biological sourceGallus gallus (Chicken)
Total number of polymer chains1
Total formula weight8136.35
Authors
Kutyshenko, N.P.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Gushchina, L.V.,Khristoforov, V.S.,Filimonov, V.V. (deposition date: 2008-04-10, release date: 2009-04-28, Last modification date: 2024-05-15)
Primary citationKutyshenko, V.P.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Gushchina, L.V.,Khristoforov, V.S.,Filimonov, V.V.,Uversky, V.N.
Solution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-"Bergeracs".
Biochim.Biophys.Acta, 1794:1813-1822, 2009
Cited by
PubMed Abstract: Two chimeric proteins, SHcapital EN, Cyrillic and SHA of the "SH3-Bergerac" family (where the beta-turn N47D48 in spectrin SH3 domain was substituted for KITVNGKTYE or KATANGKTYE sequences, respectively), were analyzed by high-resolution NMR to resolve their spatial structures and to analyze their dynamics. Although the presence of a stable beta-hairpin in the region of the insertion was confirmed, the introduced extension of the polypeptide chain in SHcapital EN, Cyrillic (approximately 17%) practically did not affect the total molecule topology. Interestingly, the introduced beta-hairpin had higher mobility in comparison with other protein regions. Finally, we performed a disorder prediction with the PONDR VSL2 algorithm and discovered that the inserted beta-hairpin in both SHH and SHA proteins exhibited significant propensity for intrinsic disorder and therefore for high mobility. In agreement with the experimental data, the predisposition for the increased intramolecular mobility was noticeably higher in SHA.
PubMed: 19732853
DOI: 10.1016/j.bbapap.2009.08.021
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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