3HCK

NMR ensemble of the uncomplexed human HCK SH2 domain, 20 structures

Summary for 3HCK

• Entry DOI: 10.2210/pdb3hck/pdb
• Descriptor: HCK SH2 (1 entity in total)
• Functional Keywords: hck, sh2, tyrosine kinase, signal transduction, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Isoform p59-HCK: Membrane; Lipid-anchor. Isoform p60-HCK: Membrane; Lipid-anchor: P08631
• Total number of polymer chains: 1
• Total formula weight: 12240.82

Authors

Zhang, W.,Smithgall, T.E.,Gmeiner, W.H. (deposition date: 1997-03-31, release date: 1997-10-15, Last modification date: 2024-05-22)

Primary citation

Zhang, W.,Smithgall, T.E.,Gmeiner, W.H.
Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase.
FEBS Lett., 406:131-135, 1997

PubMed Abstract: The hematopoietic cellular kinase (Hck) is a member of the Src family of non-receptor protein-tyrosine kinases and participates in signal transduction events regulating the growth, differentiation and function of phagocytes. The secondary structure of the SH2 domain for Hck was determined for a 13C/15N-enriched sample using multi-dimensional NMR spectroscopy. The secondary structure for the domain was determined from chemical shift indices [1H alpha, 13C alpha and 13C'], sequential NOEs [d(alphaN)(i, i+1) and d(NN)(i, i+1)], and 3J(alphaN) scalar coupling constants. The Hck SH2 domain consists of two alpha-helices and seven beta-strands. Complementary strands of beta-sheets were identified from long-range NOEs using a novel 3D, 13C/15N-edited HMQC-NOESY-(HCACO)NH experiment that correlated 1H alpha resonances between beta-strands. The secondary structure for Hck SH2 is similar to that predicted from the sequence alignment of the Src-family protein tyrosine kinases.

PubMed: 9109402
DOI: 10.1016/S0014-5793(97)00255-X

Experimental method

SOLUTION NMR