1hom

<StructureSection load='1hom' size='340' side='right'caption='[[1hom]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1hom]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HOM FirstGlance]. <br>

</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=1hom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hom OCA], [https://pdbe.org/1hom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hom RCSB], [https://www.ebi.ac.uk/pdbsum/1hom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hom ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/ANTP_DROME ANTP_DROME]] Sequence-specific transcription factor which is part of a developmental regulatory system that regulates segmental identity in the mesothorax. Provides cells with specific positional identities on the anterior-posterior axis.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution is described. The techniques used are 1H nuclear magnetic resonance spectroscopy for the data collection, and calculation of the protein structure with the program DISMAN followed by restrained energy minimization with a modified version of the program AMBER. A group of 19 conformers characterizes a well-defined structure for residues 7 to 59, with an average root-mean-square distance from the backbone atoms of 0.6 A relative to the mean of the 19 structures. The structure contains a helix from residues 10 to 21, a helix-turn-helix motif from residues 28 to 52, which is similar to those reported for several prokaryotic repressor proteins, and a somewhat flexible fourth helix from residues 53 to 59, which essentially forms an extension of the presumed recognition helix, residues 42 to 52. The helices enclose a structurally well-defined molecular core of hydrophobic amino acid side-chains.

Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy.,Billeter M, Qian Y, Otting G, Muller M, Gehring WJ, Wuthrich K J Mol Biol. 1990 Jul 5;214(1):183-97. PMID:2164583<ref>PMID:2164583</ref>

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

</div>

<div class="pdbe-citations 1hom" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Drome]]

[[Category: Billeter, M]]

[[Category: Gehring, W J]]

[[Category: Muller, M]]

[[Category: Otting, G]]

[[Category: Qian, Y Q]]

[[Category: Wuthrich, K]]

[[Category: Dna-binding protein]]