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[[Image:1ifc.jpg|left|200px]]


{{Structure
==REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION==
|PDB= 1ifc |SIZE=350|CAPTION= <scene name='initialview01'>1ifc</scene>, resolution 1.19&Aring;
<StructureSection load='1ifc' size='340' side='right'caption='[[1ifc]], [[Resolution|resolution]] 1.19&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1ifc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IFC FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.19&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ifc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ifc OCA], [https://pdbe.org/1ifc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ifc RCSB], [https://www.ebi.ac.uk/pdbsum/1ifc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ifc ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ifc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ifc OCA], [http://www.ebi.ac.uk/pdbsum/1ifc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ifc RCSB]</span>
[https://www.uniprot.org/uniprot/FABPI_RAT FABPI_RAT] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor (By similarity).
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/if/1ifc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=1ifc ConSurf].
<div style="clear:both"></div>


'''REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION'''
==See Also==
 
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The three-dimensional structure of the 131-residue rat intestinal fatty acid-binding protein, without bound ligand (apoI-FABP), has been refined with x-ray diffraction data to a nominal resolution of 1.19 A. The final model has a conventional crystallographic R-factor of 16.9% for 34,290 unique reflections [a root mean square (r.m.s.) deviation for bond length of 0.012 A and a r.m.s. deviation of 2.368 degrees for bond angles]. Ninety-two residues are present as components of the protein's 10 anti-parallel beta-strands while 14 residues are part of its two short alpha-helices. The beta-strands and alpha-helices are organized into two nearly orthogonal beta-sheets. Particular attention has been placed in defining solvent structure and the structures of discretely disordered groups in this protein. Two hundred thirty-seven solvent molecules have been identified; 24 are located within apoI-FABP. The refined model includes alternate conformers for 228 protein atoms (109 main-chain, 119 side-chain) and 63 solvent molecules. We have found several aromatic side-chains with multiple conformations located near, or in, the protein's ligand binding site. This observation, along with the fact that these side-chains have a temperature factor that is relatively higher than that of other aromatic residues, suggests that they may be involved in the process of noncovalent binding of fatty acid. The absence of a true hydrophobic core in I-FABP suggests that its structural integrity may be maintained primarily by a hydrogen bonding network involving protein and solvent atoms.
[[Category: Large Structures]]
 
==About this Structure==
1IFC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFC OCA].
 
==Reference==
Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2-A resolution., Scapin G, Gordon JI, Sacchettini JC, J Biol Chem. 1992 Feb 25;267(6):4253-69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1740465 1740465]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Gordon JI]]
[[Category: Gordon, J I.]]
[[Category: Sacchettini JC]]
[[Category: Sacchettini, J C.]]
[[Category: Scapin G]]
[[Category: Scapin, G.]]
[[Category: lipid-binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:19:03 2008''

Latest revision as of 10:34, 7 February 2024

REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTIONREFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION

Structural highlights

1ifc is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.19Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABPI_RAT FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ifc, resolution 1.19Å

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