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| - | [[Image:1ifc.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ifc| PDB=1ifc | SCENE= }} | | {{STRUCTURE_1ifc| PDB=1ifc | SCENE= }} |
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| - | '''REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION'''
| + | ===REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_1740465}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 1740465 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_1740465}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Scapin, G.]] | | [[Category: Scapin, G.]] |
| | [[Category: Lipid-binding protein]] | | [[Category: Lipid-binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:56:39 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:53:12 2008'' |
Revision as of 07:53, 1 July 2008
Template:STRUCTURE 1ifc
REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 1740465
About this Structure
1IFC is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from 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:1740465
Page seeded by OCA on Tue Jul 1 10:53:12 2008
