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Sandbox ggc6

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== Structure ==
== Structure ==
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Between the different know FABP the amino acid sequence varies widely but the three dimensional sequence is heavily conserved. <scene name='75/752265/Secondary_structures/1'>Secondary structures</scene>: It consist of ten antiparallel β strands and two short α helices. The ten antiparallel β strands are
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The FABP genes each have 4 exons and 3 introns with many residing in the same chromosomal region. Between the different know FABP the amino acid sequence varies widely but the three dimensional sequence is heavily conserved. <scene name='75/752265/Secondary_structures/1'>Secondary structures</scene>: It consist of ten antiparallel β strands and two short α helices. The ten antiparallel β strands are arranged into two nearly orthogonal 5-stranded β sheets that surround the interior binding cavity. B-FABP is commonly bound to poly-unsaturated fatty acids; this gives the ligand in the binding region a <scene name='75/752265/Ligand_ball_and_stick/1'>U-Shaped</scene> confirmation.
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arranged into two nearly orthogonal 5-stranded β sheets that surround the interior binding cavity.
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== Structural highlights ==
== Structural highlights ==

Revision as of 01:06, 23 April 2018

CRYSTAL STRUCTURE OF HUMAN BRAIN FATTY ACID BINDING PROTEIN OLEIC ACID

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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

Contents

Function

One of nine known FABP, members of the superfamily of lipid-binding proteins, that are believed to be involved in fatty acid uptake, transport, and metabolism.

Structure

The FABP genes each have 4 exons and 3 introns with many residing in the same chromosomal region. Between the different know FABP the amino acid sequence varies widely but the three dimensional sequence is heavily conserved. : It consist of ten antiparallel β strands and two short α helices. The ten antiparallel β strands are arranged into two nearly orthogonal 5-stranded β sheets that surround the interior binding cavity. B-FABP is commonly bound to poly-unsaturated fatty acids; this gives the ligand in the binding region a confirmation.

Structural highlights

Color Key: Cyan-Alpha Helix; Magenta-Beta Sheet; Yellow-Arg 514; Lime Green-All Glutamate; Dark Blue-Backbone/Main Chain; Maroon-All Lys; Black-Ser509; Orange-Cys502. The N-free pyrazole of 22 interacts with Glu500 and Cys502 in the hinge region by two hydrogen bonds [3]. . </StructureSection>

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ Tomita N, Hayashi Y, Suzuki S, Oomori Y, Aramaki Y, Matsushita Y, Iwatani M, Iwata H, Okabe A, Awazu Y, Isono O, Skene RJ, Hosfield DJ, Miki H, Kawamoto T, Hori A, Baba A. Structure-based discovery of cellular-active allosteric inhibitors of FAK. Bioorg Med Chem Lett. 2013 Mar 15;23(6):1779-85. doi: 10.1016/j.bmcl.2013.01.047., Epub 2013 Jan 26. PMID:23414845 doi:http://dx.doi.org/10.1016/j.bmcl.2013.01.047
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