PDBsum entry 3hck

Transferase

PDB id: 3hck

Contents

Protein chain

107 a.a. *

* Residue conservation analysis

PDB id:

3hck

Name:

Transferase

Title:

Nmr ensemble of the uncomplexed human hck sh2 domain, 20 structures

Structure:

Hck sh2. Chain: a. Fragment: sh2, residues 119 - 224 of human hck. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Gene: residues e119-k224 of human hc. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

W.Zhang,T.E.Smithgall,W.H.Gmeiner

Key ref:

W.Zhang et al. (1997). Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase. Febs Lett, 406, 131-135. PubMed id: 9109402 DOI: 10.1016/S0014-5793(97)00255-X

Date:

31-Mar-97 Release date: 15-Oct-97

Protein chain

P08631  (HCK_HUMAN) -  Tyrosine-protein kinase HCK from Homo sapiens

Seq: 526 a.a.

Struc: 107 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.7.10.2 - non-specific protein-tyrosine kinase.
• Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/S0014-5793(97)00255-X

Febs Lett 406:131-135 (1997)

PubMed id: 9109402

Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase.

W.Zhang, T.E.Smithgall, W.H.Gmeiner.

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.

Selected figure(s)

Figure 1.
Fig. 1. Pulse sequence of the 3D ^13C/^15N-edited HMQC-NOESY-(HCACO)NH experiment. Narrow and wide bars represent 90° and 180° pulses, respectively. All pulses are applied along the x-axis unless otherwise indicated. ^13C′ decoupling was achieved using the SEDUCE-1 modulation [45] at an RF field strength of 840 Hz. ^15N decoupling was accomplished using a WALTZ-16 scheme [46]. The phase cycle is φ1=x, -x; φ2=2x, 2(-x); φ3=4x, 4(-x); φ4=8x, 8(-x); receiver=x, 2(-x), x, -x, 2x, 2(-x), 2x, -x, x, 2(-x), x. Quadrature detection in t[1] and t[2] is achieved using the States-TPPI method [47] by incrementing the phases of φ1 and φ4, independently. All other parameters are similar to those described for the 3D ^15N-edited NOESY-(HCACO)NH experiment [31].

Figure 2.
Fig. 2. ^15N HSQC spectrum of ^15N-labeled Hck SH2, showing assignment of amide resonances. Backbone resonances are labeled with the residue name followed by residue number in the sequence. Side chain NH of Trp and Arg are indicated with NH while side chain NH[2] of Asn and Gln are indicated by NH[2].

The above figures are reprinted by permission from the Federation of European Biochemical Societies: Febs Lett (1997, 406, 131-135) copyright 1997.

Figures were selected by an automated process.