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The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes.

Abstract:

HMGB1 (high mobility group B1) is a conserved chromosomal protein composed of two similar DNA binding domains (HMG box A and box B) linked by a short basic stretch to an acidic C-terminal tail of 30 residues. The acidic tail modulates the DNA binding properties of HMGB1, and its length differentiates the various HMGB family members. We synthesized a peptide that corresponds to the acidic tail in HMGB1 (T-peptide) and studied its binding to the single boxes and to the fragment corresponding to...

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Publication status:
Published

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Publisher copy:
10.1021/bi049364k

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
Journal:
Biochemistry More from this journal
Volume:
43
Issue:
38
Pages:
11992-11997
Publication date:
2004-09-01
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Language:
English
Keywords:
Pubs id:
pubs:374149
UUID:
uuid:6e2bb26e-91b4-4715-b58d-4f4e08f56d05
Local pid:
pubs:374149
Source identifiers:
374149
Deposit date:
2013-11-16

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