The basic folding topology of SH3 domain consists of: two 3-stranded beta-sheets packed orthogonally against each other to form a single htdrophobic core. Within the sheets, strands are joined by the RT, n-src, distal loops, while the crossovers between the two sheets occur at a diverging type II beta-turn and a short 310-helix. (Figure adopted from Grantcharova et al., Natu. Struct. Biol., 1998, 5(8):714)

Hydrophobic core structure. The hydrophobic core of src-SH3 domain can be devided into to calsses, 1st [orange]: Ala45, Ile34, Leu 32, Ile 56 (mutations of these sites affect the folding rate significantly); 2nd [yellow]: Phe 10, Leu24, Tyr 16, Val 61 (these residues are partially solvent exposed, and they affect little to the folding rate)

[Comparison of SH3_Domains][Home]

Danny S. Hsu 1999-2000. All rights reserved.