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1jjj

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[[Image:1jjj.gif|left|200px]]
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{{STRUCTURE_1jjj| PDB=1jjj | SCENE= }}
{{STRUCTURE_1jjj| PDB=1jjj | SCENE= }}
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'''SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN'''
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===SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN===
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==Overview==
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Human epidermal-type fatty acid-binding protein (E-FABP) belongs to a family of intracellular 14-15 kDa lipid-binding proteins, whose functions have been associated with fatty acid signalling, cell growth, regulation and differentiation. As a contribution to understanding the structure-function relationship, we report in the present study features of its solution structure and backbone dynamics determined by NMR spectroscopy. Applying multi-dimensional high-resolution NMR techniques on unlabelled and 15N-enriched recombinant human E-FABP, the 1H and 15N resonance assignments were completed. On the basis of 2008 distance restraints, the three-dimensional solution structure of human E-FABP was subsequently obtained (backbone atom root-mean-square deviation of 0.92+/-0.11 A; where 1 A=0.1 nm), consisting mainly of 10 anti-parallel beta-strands that form a beta-barrel structure. 15N relaxation experiments (T1, T2 and heteronuclear nuclear Overhauser effects) at 500, 600 and 800 MHz provided information on the internal dynamics of the protein backbone. Nearly all non-terminal backbone amide groups showed order parameters S(2)&gt;0.8, with an average value of 0.88+/-0.04, suggesting a uniformly low backbone mobility in the nanosecond-to-picosecond time range. Moreover, hydrogen/deuterium exchange experiments indicated a direct correlation between the stability of the hydrogen-bonding network in the beta-sheet structure and the conformational exchange in the millisecond-to-microsecond time range. The features of E-FABP backbone dynamics elaborated in the present study differ markedly from those of the phylogenetically closely related heart-type FABP and the more distantly related ileal lipid-binding protein, implying a strong interdependence with the overall protein stability and possibly also with the ligand-binding affinity for members of the lipid-binding protein family.
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(as it appears on PubMed at http://www.pubmed.gov), where 12049637 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12049637}}
==About this Structure==
==About this Structure==
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1JJJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJJ OCA].
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1JJJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJJ OCA].
==Reference==
==Reference==
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[[Category: Holo form]]
[[Category: Holo form]]
[[Category: Nmr spectroscopy]]
[[Category: Nmr spectroscopy]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:18:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:20:35 2008''

Revision as of 17:20, 1 July 2008

Image:1jjj.png

Template:STRUCTURE 1jjj

SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN

Template:ABSTRACT PUBMED 12049637

About this Structure

1JJJ is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP)., Gutierrez-Gonzalez LH, Ludwig C, Hohoff C, Rademacher M, Hanhoff T, Ruterjans H, Spener F, Lucke C, Biochem J. 2002 Jun 15;364(Pt 3):725-37. PMID:12049637

Page seeded by OCA on Tue Jul 1 20:20:35 2008

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