2hmb

<StructureSection load='2hmb' size='340' side='right' caption='[[2hmb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

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

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></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=2hmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmb OCA], [http://pdbe.org/2hmb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hmb RCSB], [http://www.ebi.ac.uk/pdbsum/2hmb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hmb ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/FABPH_HUMAN FABPH_HUMAN]] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/2hmb_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The three-dimensional structure of recombinant human muscle fatty acid-binding protein with a bound fatty acid has been solved and refined with x-ray diffraction data to 2.1 A resolution. The refined model has a crystallographic R factor of 19.5% for data between 9.0 and 2.1 A (7243 unique reflections) and root-mean-square deviations in bond length and bond angle of 0.013 A and 2.7 degrees. The protein contains 10 antiparallel beta-strands and two short alpha-helices which are arranged into two approximately orthogonal beta-sheets. Difference electron density maps and a multiple isomorphous derivative electron density map showed the presence of a single bound molecule of a long chain fatty acid within the interior core of the protein. The hydrocarbon tail of the fatty acid was found to be in a "U-shaped" conformation. Seven ordered water molecules were also identified within the interior of the protein in a pocket on the pseudo-si face of the fatty acid's bent hydrocarbon tail. The methylene tail of the fatty acid forms van der Waals interactions with atoms from 13 residues and three ordered waters. The carboxylate of the fatty acid is located in the interior of the protein where it forms hydrogen bonds with the side chains of Tyr128 and Arg126 and two ordered water molecules. A comparison of the three-dimensional structure of human muscle fatty acid-binding protein and rat intestinal fatty acid-binding protein shows strong similarity. Both proteins bind a single fatty acid within their interior cores, but the bound fatty acids are very different in their conformations and interactions. These findings suggest that the intestinal and muscle fatty acid-binding proteins have evolved distinct binding sites in order to satisfy different requirements within the tissues where they are expressed.

Three-dimensional structure of recombinant human muscle fatty acid-binding protein.,Zanotti G, Scapin G, Spadon P, Veerkamp JH, Sacchettini JC J Biol Chem. 1992 Sep 15;267(26):18541-50. PMID:1526991<ref>PMID:1526991</ref>

 

[[Category: Human]]

[[Category: Sacchettini, J C]]

[[Category: Scapin, G]]

[[Category: Spadon, P]]

[[Category: Veerkamp, J H]]

[[Category: Zanotti, G]]

[[Category: Lipid-binding protein]]