2kr3 is a 1 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Protein SHA-D of "SH3-Bergerac" chimeric proteins family was constructed by substitution of beta-turn N47-D48 in spectrin SH3-domain by KATANDKTYE amino acid sequence. Structural and dynamics properties of SHA-D in solution were studied by with the help of high-resolution NMR. The extension of SHA-D polypeptide chain in comparison with wild type of protein WT-SH3 (~ 17%) practically doesn't affect almost the total molecule topology. 3D-structure of SHA-D is practically identical to the proteins of "SH3-Bergerac" family. However there are some differences in dynamic characteristics in the region of substitution. The G52D substitution in SHA-D protein results in a destabilization of the region insertion where the conditions for conformational exchange appear. Destabilization further affects the entire SHA- D molecule making its structure more labile.
[Chimeric SHA-D domain ("SH3-Bergerac"): 3D-structure and dynamics studies in solution],Khristophorov VS, Prokhorov DA, Timchenko MA, Kudrevatykh IuA, Gushchina LV, Filimonov VV, Kutyshenko VP Bioorg Khim. 2010 Jul-Aug;36(4):505-13. PMID:20823919[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
