2RMO

Solution structure of alpha-spectrin_SH3-bergerac from Chicken

Summary for 2RMO

• Entry DOI: 10.2210/pdb2rmo/pdb
• NMR Information: BMRB: 11026
• Descriptor: Spectrin alpha chain, brain (1 entity in total)
• Functional Keywords: sh3, bergerac, actin capping, actin-binding, calcium, calmodulin-binding, cytoplasm, cytoskeleton, membrane, phosphorylation, sh3 domain, signaling protein
• Biological source: Gallus gallus (chicken)
• Cellular location: Cytoplasm, cytoskeleton: P07751
• Total number of polymer chains: 1
• Total formula weight: 8066.22

Authors

Kutyshenko, V.P.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Fedyukina, D.V.,Gushchina, L.V.,Khristoforov, V.S.,Filimonov, V.V. (deposition date: 2007-11-07, release date: 2008-09-30, Last modification date: 2024-05-29)

Primary citation

Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Fedyukina, D.V.,Gushchina, L.V.,Khristoforov, V.S.,Filimonov, V.V.,Kutyshenko, V.P.
Study of the structure and dynamics of a chimeric variant of the SH3 domain (SHA-Bergerac) by NMR spectroscopy
Russ.J.Bioorganic Chem., 34:578-585, 2008

PubMed Abstract: A structural-dynamic study of one of the chimeric proteins (SHA) belonging to the SH3-Bergerac family and containing the KATANGKTYE sequence instead of the N47D48 beta-turn in the spectrin SH3 domain was carried out by high resolution NMR spectroscopy. The spatial structure of the protein was determined and its dynamics in solution was investigated on the basis of the NMR data. The elongation of the SHA polypeptide chain in comparison with the WT-SH3 original protein (by ~17%) exerts practically no effect on the general topology of the molecule. The presence of a stable beta-hairpin in the region of insertion was confirmed. This hairpin was shown to have a higher mobility in comparison with other regions of the protein.

PubMed: 19060939
DOI: 10.1134/S1068162008050075

Experimental method

SOLUTION NMR