PMID- 10329173
OWN - NLM
STAT- MEDLINE
DCOM- 19990609
LR  - 20111117
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 288
IP  - 4
DP  - 1999 May 14
TI  - The solution structure of the homeodomain of the rat insulin-gene enhancer
      protein isl-1. Comparison with other homeodomains.
PG  - 689-703
AB  - Homeodomains are one of the key families of eukaryotic DNA-binding motifs and
      provide an important model system for DNA recognition. We have determined a
      high-quality nuclear magnetic resonance (NMR) structure of the DNA-binding
      homeodomain of the insulin gene enhancer protein Isl-1 (Isl-1-HD). It forms the
      first solution structure of a homeodomain from the LIM family. It contains a
      well-defined inner core (residues 12-55) consisting of the classical three-helix 
      structure observed in other homeodomains. The N terminus is unstructured up to
      residue 8, while the C terminus gradually becomes unstructured from residue 55
      onwards. Some flexibility is evident in the loop parts of the inner core.
      Isl-1-HD has, despite its low sequence identity (23-34 %), a structure that is
      strikingly similar to that of the other homeodomains with known three-dimensional
      structures. Detailed analysis of Isl-1-HD and the other homeodomains rationalizes
      the differences in their temperature stability and explains the low stability of 
      the Isl-1-HD in the free state (tm 22-30 degrees C). Upon DNA binding, a
      significant stabilization occurs (tm>55 degrees C). The low stability of Isl-1-HD
      (and other mammalian homeodomains) suggests that in vivo Isl-1-HD recognizes its 
      cognate DNA from its unfolded state.
CI  - Copyright 1999 Academic Press.
FAU - Ippel, H
AU  - Ippel H
AD  - Department of Medical Biochemistry and Biophysics, Umea University, Umea, S 901
      87, Sweden.
FAU - Larsson, G
AU  - Larsson G
FAU - Behravan, G
AU  - Behravan G
FAU - Zdunek, J
AU  - Zdunek J
FAU - Lundqvist, M
AU  - Lundqvist M
FAU - Schleucher, J
AU  - Schleucher J
FAU - Lycksell, P O
AU  - Lycksell PO
FAU - Wijmenga, S
AU  - Wijmenga S
LA  - eng
SI  - PDB/1BW5
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Homeodomain Proteins)
RN  - 0 (LIM-Homeodomain Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (insulin gene enhancer binding protein Isl-1)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Crystallography, X-Ray
MH  - Homeodomain Proteins/*chemistry
MH  - LIM-Homeodomain Proteins
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - *Nerve Tissue Proteins
MH  - Protein Conformation
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Transcription Factors
EDAT- 1999/05/18 00:00
MHDA- 1999/05/18 00:01
CRDT- 1999/05/18 00:00
PHST- 1999/05/18 00:00 [pubmed]
PHST- 1999/05/18 00:01 [medline]
PHST- 1999/05/18 00:00 [entrez]
AID - S0022-2836(99)92718-3 [pii]
AID - 10.1006/jmbi.1999.2718 [doi]
PST - ppublish
SO  - J Mol Biol. 1999 May 14;288(4):689-703. doi: 10.1006/jmbi.1999.2718.