Lan-Hsiang Wang
National Institutes of Health
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Publication
Featured researches published by Lan-Hsiang Wang.
Journal of Biological Chemistry | 1998
Solly Weiler; James M. Gruschus; Desiree H. H. Tsao; Lei Yu; Lan-Hsiang Wang; Marshall W. Nirenberg; James A. Ferretti
Secondary structures, DNA binding properties, and thermal denaturation behavior of six site-directed mutant homeodomains encoded by the vnd/NK-2 gene from Drosophila melanogaster are described. Three single site H52R, Y54M, and T56W mutations, two double site H52R/T56W and Y54M/T56W mutations, and one triple site H52R/Y54M/T56W mutation were investigated. These positions were chosen based on their variability across homeodomains displaying differences in secondary structure and DNA binding specificity. Multidimensional NMR, electrophoretic mobility shift assays, and circular dichroism spectropolarimetry studies were carried out on recombinant 80-amino acid residue proteins containing the homeodomain. Position 56, but more importantly position 56 in combination with position 52, plays an important role in determining the length of the recognition helix. The H52R mutation alone does not affect the length of this helix but does increase the thermal stability. Introduction of site mutations at positions 52 and 56 in vnd/NK-2 does not modify their high affinity binding to the 18-base pair DNA fragment containing the vnd/NK-2 consensus binding sequence, CAAGTG. Site mutations involving position 54 (Y54M, Y54M/T56W, and H52R/Y54M/T56W) all show a decrease of 1 order of magnitude in their binding affinity. The roles in structure and sequence specificity of individual atom-atom interactions are described.
Proceedings of the National Academy of Sciences of the United States of America | 2002
Lan-Hsiang Wang; Rebecca Chmelik; Marshall W. Nirenberg
The ventral nervous system defective (vnd)/NK-2 homeodomain and some flanking amino acid residues were expressed in Escherichia coli, purified to homogeneity, and the protein was covalently coupled to Sepharose. Oligodeoxynucleotides that contained 16-bp random sequences were purified by vnd/NK-2 affinity column chromatography, cloned, and sequenced. The consensus nucleotide sequence of the vnd/NK-2 homeodomain binding site was shown to be T(T/C)AAGTG(G/C). The apparent equilibrium dissociation constant (KD) of the vnd/NK-2 homeodomain for the consensus sequence is 1.9 × 10−10 M. In addition, results of competition between oligodeoxynucleotides for binding to the vnd/NK-2 homeodomain and determination of the apparent KD values of oligodeoxynucleotides that differ from the consensus sequence by only a single base pair demonstrate that the four central nucleotides, AAGT, in this sequence play a major role in determining the affinity of binding.
Biochemistry | 1997
James M. Gruschus; Desiree H. H. Tsao; Lan-Hsiang Wang; Marshall W. Nirenberg; James A. Ferretti
Biochemistry | 1994
Desiree H. H. Tsao; James M. Gruschus; Lan-Hsiang Wang; Marshall W. Nirenberg; James A. Ferretti
Journal of Molecular Biology | 1995
Desiree H. H. Tsao; James M. Gruschus; Lan-Hsiang Wang; Marshall W. Nirenberg; James A. Ferretti
Journal of Molecular Biology | 1999
James M. Gruschus; Desiree H. H. Tsao; Lan-Hsiang Wang; Marshall W. Nirenberg; James A. Ferretti
Annals of the New York Academy of Sciences | 1995
Marshall W. Nirenberg; Kohzo Nakayama; Noriko Nakayama; Yongsok Kim; Dervla M. Mellerick; Lan-Hsiang Wang; Keith O. Webber; Rajnikant Lad
Proceedings of the National Academy of Sciences of the United States of America | 2005
Lan-Hsiang Wang; Rebecca Chmelik; Derek Ng Tang; Marshall W. Nirenberg
Archive | 2002
Lan-Hsiang Wang; Rebecca Chmelik; Marshall W. Nirenberg
Journal of Molecular Biology | 1999
James M. Gruschus; Desiree H. H. Tsao; Lan-Hsiang Wang; Marshall W. Nirenberg; James A. Ferretti