Ternary complex of an Crk SH2 domain, Crk-derived phophopeptide, and Abl SH3 domain by NMR spectroscopy
Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide
PROTO-ONCOGENE C-CRK, ADAPTER MOLECULE CRK, P38
SWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGD QEFDSLPALLEFYKIHYLDTTTLIEPVSR
1AWO contains NMR structure of Abl SH3 domain in an SH(32) fragment
1BBZ contains Crystal structure of Abl SH3 domain with high-affinity ligand
2ABL contains Sh3-Sh2 Domain Fragment Of Human Bcr-Abl Tyrosine Kinase
1AYA contains Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase.
2PLD contains Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-1 complexed with a high affinity binding peptide.
1SPS contains Crystal structure of the Src SH2 in complex with YEEI
Intermolecular distance restraints were obtained from reverse half-filtered 2D- and 3D-NOESY spectra (300 ms mixing time) on sample in 99% D2O. Methyl prochiral assignments were made on a 10% 13C-labeled sample according to Neri et al (Biochemistry 28:7510; 1989). HACAN and CBCA(CO)N(CA)HA experiments were used to assign the proline residues in the Crk SH2 domain according to Kanelis et al (JBNMR 16:253; 2000)
This structure represents the lowest energy solution based on 2406 SH2 intramolecular restraints, 1628 SH3 intramolecular restraints, 37 SH2-SH3 intermolecular restraints, 64 SH2-phosphopeptide intermolecular restraints, 50 hydrogen bonds, 54 direct 3J-HNHA couplings and 166 dihedral angle restraints from TALOS Residues 217-220 and 225-229 of the Crk phosphopeptide (Chain B) are disordered. As intermolecular contacts between the SH2 domain (Chain A) and the SH3 domain (Chain C) limited to amino acids 67-75 in DE-loop of the SH2 domain, there is no unique orientation between the SH2 domain and SH3 domain.
0.6-1.5mM Crk SH2 domain U-15N, 13C; 50mM sodium phosphate pH6.8, 0.02% sodium azide
Crk, SH2, Abl, SH3, adaptor protein, phosphopeptide, PROTEIN BINDING-TRANSFERASE COMPLEX