1bw5

<StructureSection load='1bw5' size='340' side='right'caption='[[1bw5]], [[NMR_Ensembles_of_Models | 50 NMR models]]' scene=''>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bw5 OCA], [https://pdbe.org/1bw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bw5 RCSB], [https://www.ebi.ac.uk/pdbsum/1bw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bw5 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/ISL2_RAT ISL2_RAT]] Transcriptional factor that defines subclasses of motoneurons that segregate into columns in the spinal cord and select distinct axon pathways (By similarity).

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== Publication Abstract from PubMed ==

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&gt;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.

The solution structure of the homeodomain of the rat insulin-gene enhancer protein isl-1. Comparison with other homeodomains.,Ippel H, Larsson G, Behravan G, Zdunek J, Lundqvist M, Schleucher J, Lycksell PO, Wijmenga S J Mol Biol. 1999 May 14;288(4):689-703. PMID:10329173<ref>PMID:10329173</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Behravan, G]]

[[Category: Ippel, J H]]

[[Category: Larsson, G]]

[[Category: Lundqvist, M]]

[[Category: Lycksell, P O]]

[[Category: Schleucher, J]]

[[Category: Wijmenga, S S]]

[[Category: Zdunek, J]]

[[Category: Lim domain]]