1jjx
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Human brain-type fatty acid-binding protein (B-FABP) has been | + | Human brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and 15N-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the 1H and 15N resonances were achieved by applying multidimensional homo- and heteronuclear NMR experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a total of 2490 meaningful distance constraints. The overall B-FABP structure exhibits the typical backbone conformation described for other members of the FABP family, consisting often antiparallel beta-strands (betaA to betaJ) that form two almost orthogonal beta-sheets, a helix-turn-helix motif that closes the beta-barrel on one side, and a short N-terminal helical loop. A comparison with the crystal structure of the same protein complexed with docosahexaenoic acid reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity. |
==Disease== | ==Disease== | ||
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[[Category: Rademacher, M.]] | [[Category: Rademacher, M.]] | ||
[[Category: Rueterjans, H.]] | [[Category: Rueterjans, H.]] | ||
| - | [[Category: Veerkamp, J | + | [[Category: Veerkamp, J H.]] |
| - | [[Category: Zimmerman, A | + | [[Category: Zimmerman, A W.]] |
[[Category: 15n isotope enrichment]] | [[Category: 15n isotope enrichment]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
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[[Category: nmr spectroscopy]] | [[Category: nmr spectroscopy]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:30 2008'' |
Revision as of 11:23, 21 February 2008
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Solution Structure of Recombinant Human Brain-type Fatty acid Binding Protein
Contents |
Overview
Human brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and 15N-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the 1H and 15N resonances were achieved by applying multidimensional homo- and heteronuclear NMR experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a total of 2490 meaningful distance constraints. The overall B-FABP structure exhibits the typical backbone conformation described for other members of the FABP family, consisting often antiparallel beta-strands (betaA to betaJ) that form two almost orthogonal beta-sheets, a helix-turn-helix motif that closes the beta-barrel on one side, and a short N-terminal helical loop. A comparison with the crystal structure of the same protein complexed with docosahexaenoic acid reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity.
Disease
Known diseases associated with this structure: Infundibular hypoplasia and hypopituitarism OMIM:[313430], Mental retardation, X-linked, with isolated growth hormone deficiency OMIM:[313430]
About this Structure
1JJX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of fatty acid-binding protein from human brain., Rademacher M, Zimmerman AW, Ruterjans H, Veerkamp JH, Lucke C, Mol Cell Biochem. 2002 Oct;239(1-2):61-8. PMID:12479569
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