東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Biophysical characterization of zinc...

Davis, Alisa M.

Linked to FindBook

Google Book

Amazon

博客來

Biophysical characterization of zinc(II)-binding domains in two systems: Neural zinc finger factor-1 and T-cell co-receptors DC4 and DC8 alpha with T-cell-specific kinase Lck.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Biophysical characterization of zinc(II)-binding domains in two systems: Neural zinc finger factor-1 and T-cell co-receptors DC4 and DC8 alpha with T-cell-specific kinase Lck./
Author:	Davis, Alisa M.
Description:	145 p.
Notes:	Adviser: Jeremy M. Berg.
Contained By:	Dissertation Abstracts International67-11B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3240694
ISBN:	9780542954023

Biophysical characterization of zinc(II)-binding domains in two systems: Neural zinc finger factor-1 and T-cell co-receptors DC4 and DC8 alpha with T-cell-specific kinase Lck.
Davis, Alisa M.

Biophysical characterization of zinc(II)-binding domains in two systems: Neural zinc finger factor-1 and T-cell co-receptors DC4 and DC8 alpha with T-cell-specific kinase Lck. - 145 p.

Adviser: Jeremy M. Berg.

Thesis (Ph.D.)--The Johns Hopkins University, 2007.

The first zinc(II)-binding domain described in transcription factors contains a CCHH motif. Transcription factors characterized by a CCHC zinc(II)-binding motif have also been identified, including Neural Zinc Finger Factor 1 (NZF-1). NZF-1 contains six zinc(II)-binding domains with a CCHHC motif. Domains two and three specifically bind the beta-retinoic acid response element DNA sequence. Previous NMR structural studies indicate the second conserved histidine of the motif is involved in stabilizing stacking interactions rather than metal binding. Substitution of phenylalanine for this histidine in a two-domain construct results in metal-binding affinity similar to wild type, but diminished DNA-binding affinity. In addition, comparison of the 1D 1H NMR spectra of the wild type and variant proteins reveals the protein does not fold properly without the second histidine. These results indicate the conserved non-metal-binding His must serve a structural role other than stacking. Lead(II) can bind to this metal site and disrupt DNA binding; however, the domain has at least two orders of magnitude less affinity for Pb(II) than Zn(II).

ISBN: 9780542954023Subjects--Topical Terms:

1019105
Biophysics, General.

Biophysical characterization of zinc(II)-binding domains in two systems: Neural zinc finger factor-1 and T-cell co-receptors DC4 and DC8 alpha with T-cell-specific kinase Lck.
LDR:03326nam 2200289 a 45 001 967402
005 20110915
008 110915s2007 eng d
020 $a 9780542954023
035 $a (UMI)AAI3240694
035 $a AAI3240694
040 $a UMI $c UMI
100 1 $a Davis, Alisa M. $3 1291279
245 1 0 $a Biophysical characterization of zinc(II)-binding domains in two systems: Neural zinc finger factor-1 and T-cell co-receptors DC4 and DC8 alpha with T-cell-specific kinase Lck.
300 $a 145 p.
500 $a Adviser: Jeremy M. Berg.
500 $a Source: Dissertation Abstracts International, Volume: 67-11, Section: B, page: 6246.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2007.
520 $a The first zinc(II)-binding domain described in transcription factors contains a CCHH motif. Transcription factors characterized by a CCHC zinc(II)-binding motif have also been identified, including Neural Zinc Finger Factor 1 (NZF-1). NZF-1 contains six zinc(II)-binding domains with a CCHHC motif. Domains two and three specifically bind the beta-retinoic acid response element DNA sequence. Previous NMR structural studies indicate the second conserved histidine of the motif is involved in stabilizing stacking interactions rather than metal binding. Substitution of phenylalanine for this histidine in a two-domain construct results in metal-binding affinity similar to wild type, but diminished DNA-binding affinity. In addition, comparison of the 1D 1H NMR spectra of the wild type and variant proteins reveals the protein does not fold properly without the second histidine. These results indicate the conserved non-metal-binding His must serve a structural role other than stacking. Lead(II) can bind to this metal site and disrupt DNA binding; however, the domain has at least two orders of magnitude less affinity for Pb(II) than Zn(II).
520 $a Recently, the "zinc clasp" was described (Kim, PW et al., Science , 301(5640), 19 Sep 2003, pp. 1725-1728). In this domain, two distinct proteins, each containing a dicysteine motif, coordinate Zn(II) in complex. The C-terminal cytosolic domains of T-cell co-receptors CD4 and CD8alpha have a CXC motif that interacts with the N-terminal CXXC motif of T-cell-specific Src-family kinase, Lck. While the heterodimer is involved in T-cell signaling, no evidence for homodimer formation has been reported. Size exclusion chromatography, 1D 1H and 19F NMR, and visible spectroscopy with Co(II) as a spectroscopic probe for Zn(II) show that each peptide does form a homodimer. Additional studies reveal heterodimers form preferentially to homodimers. The overall charge of the peptides and spacing between cysteines in the dicysteine motif were modified to study the effect on preferential heterodimer formation. Neither charge- nor cysteine spacing-modified peptides have preferential heterodimer formation relative to Lck homodimer formation. The Homo sapiens proteome was searched for similar motifs, but yielded no broad category of proteins utilizing this type of interaction.
590 $a School code: 0098.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
690 $a 0786
710 2 0 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 67-11B.
790 $a 0098
790 1 0 $a Berg, Jeremy M., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3240694