PDBsum entry 1kik

Transferase

PDB id

1kik

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Contents

			Protein chain

					57 a.a. *

* Residue conservation analysis

PDB id:

1kik

Links

Name:

Transferase

Title:

Sh3 domain of lymphocyte specific kinase (lck)

Structure:

Proto-oncogene tyrosine-protein kinase lck. Chain: a. Fragment: sh3 domain (residues 64-120). Synonym: p56-lck, lsk, t cell-specific protein-tyrosine kinase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

25 models

Authors:

L.Briese,D.Willbold

Key ref:

L.Briese and D.Willbold (2003). Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy. Bmc Struct Biol, 3, 3. PubMed id: 12734017

Date:

03-Dec-01

Release date:

12-Dec-01

PROCHECK

	Headers

	References

Protein chain

P06239 (LCK_HUMAN) - Tyrosine-protein kinase Lck from Homo sapiens

Seq: Struc:					509 a.a. 57 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.7.10.2 - non-specific protein-tyrosine kinase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

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

	Bmc Struct Biol 3:3 (2003)
PubMed id: 12734017

Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy.
L.Briese, D.Willbold.

ABSTRACT

BACKGROUND: Protein tyrosine kinases are involved in signal transduction pathways that regulate cell growth, differentiation, activation and transformation. Human lymphocyte specific kinase (Lck) is a 56 kDa protein involved in T-cell- and IL2-receptor signaling. Three-dimensional structures are known for SH3, SH2 and kinase domains of Lck as well as for other tyrosine kinases. No structure is known for the unique domain of any Src-type tyrosine kinase. RESULTS: Lck(1-120) comprising unique and SH3 domains was structurally investigated by nuclear magnetic resonance spectroscopy. We found the unique domain, in contrast to the SH3 part, to have basically no defined structural elements. The solution structure of the SH3 part could be determined with very high precision. It does not show significant differences to Lck SH3 in the absence of the unique domain. Minor differences were observed to the X-ray structure of Lck SH3. CONCLUSION: The unique domain of Lck does not contain any defined structure elements in the absence of ligands and membranes. Presence of the unique domain is not relevant to the three-dimensional structure of the Lck SH3 domain.

Literature references that cite this PDB file's key reference

PubMed id

Reference

15976924

L.Briese, A.Preusser, and D.Willbold (2005).
Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.

J Biomed Sci, 12, 451-456.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.