1lr5

<StructureSection load='1lr5' size='340' side='right' caption='[[1lr5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[1lr5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Maize Maize]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LR5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lrh|1lrh]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lr5 OCA], [http://pdbe.org/1lr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lr5 RCSB], [http://www.ebi.ac.uk/pdbsum/1lr5 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/ABP1_MAIZE ABP1_MAIZE]] This is probably a receptor for the plant hormone auxin.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/1lr5_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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

== Publication Abstract from PubMed ==

The structure of auxin-binding protein 1 (ABP1) from maize has been determined at 1.9 A resolution, revealing its auxin-binding site. The structure confirms that ABP1 belongs to the ancient and functionally diverse germin/seed storage 7S protein superfamily. The binding pocket of ABP1 is predominantly hydrophobic with a metal ion deep inside the pocket coordinated by three histidines and a glutamate. Auxin binds within this pocket, with its carboxylate binding the zinc and its aromatic ring binding hydrophobic residues including Trp151. There is a single disulfide between Cys2 and Cys155. No conformational rearrangement of ABP1 was observed when auxin bound to the protein in the crystal, but examination of the structure reveals a possible mechanism of signal transduction.

Crystal structure of auxin-binding protein 1 in complex with auxin.,Woo EJ, Marshall J, Bauly J, Chen JG, Venis M, Napier RM, Pickersgill RW EMBO J. 2002 Jun 17;21(12):2877-85. PMID:12065401<ref>PMID:12065401</ref>

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

</div>

<div class="pdbe-citations 1lr5" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Maize]]

[[Category: Bauley, J]]

[[Category: Chen, J G]]

[[Category: Marshall, J]]

[[Category: Napier, R M]]

[[Category: Pickersgill, R W]]

[[Category: Venis, M]]

[[Category: Woo, E J]]

[[Category: Protein binding]]