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6l7k

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solution structure of hIFABP V60C/Y70C variant.

Structural highlights

6l7k is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABPI_HUMAN 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.

Publication Abstract from PubMed

Fatty acid binding proteins play an important role in the transportation of fatty acids. Despite intensive studies, how fatty acids enter the protein cavity for binding is still controversial. Here, a gap-closed variant of human intestinal fatty acid binding protein was generated by mutagenesis, in which the gap is locked by a disulfide bridge. According to its structure determined here by NMR, this variant has no obvious openings as the ligand entrance and the gap cannot be widened by internal dynamics. Nevertheless, it still takes up fatty acids and other ligands. NMR relaxation dispersion, chemical exchange saturation transfer, and hydrogen-deuterium exchange experiments show that the variant exists in a major native state, two minor native-like states, and two locally unfolded states in aqueous solution. Local unfolding of either betaB-betaD or helix 2 can generate an opening large enough for ligands to enter the protein cavity, but only the fast local unfolding of helix 2 is relevant to the ligand entry process.

Ligand Entry into Fatty Acid Binding Protein via Local Unfolding Instead of Gap Widening.,Xiao T, Lu Y, Fan JS, Yang D Biophys J. 2020 Jan 21;118(2):396-402. doi: 10.1016/j.bpj.2019.12.005. Epub 2019 , Dec 14. PMID:31870540^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xiao T, Lu Y, Fan JS, Yang D. Ligand Entry into Fatty Acid Binding Protein via Local Unfolding Instead of Gap Widening. Biophys J. 2020 Jan 21;118(2):396-402. doi: 10.1016/j.bpj.2019.12.005. Epub 2019 , Dec 14. PMID:31870540 doi:http://dx.doi.org/10.1016/j.bpj.2019.12.005

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6l7k"

Categories: Homo sapiens | Large Structures | Fan J | Yang D

@@ Line 1: / Line 1: @@
 ==solution structure of hIFABP V60C/Y70C variant.==
-<StructureSection load='6l7k' size='340' side='right'caption='[[6l7k]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6l7k' size='340' side='right'caption='[[6l7k]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6l7k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L7K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6l7k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L7K FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABP2, FABPI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6l7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l7k OCA], [https://pdbe.org/6l7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l7k RCSB], [https://www.ebi.ac.uk/pdbsum/6l7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l7k ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6l7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l7k OCA], [https://pdbe.org/6l7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l7k RCSB], [https://www.ebi.ac.uk/pdbsum/6l7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l7k ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FABPI_HUMAN FABPI_HUMAN]] 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.
+[https://www.uniprot.org/uniprot/FABPI_HUMAN FABPI_HUMAN] 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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 17: @@
 </div>
 <div class="pdbe-citations 6l7k" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Fan, J]]
+[[Category: Fan J]]
-[[Category: Yang, D]]
+[[Category: Yang D]]
-[[Category: Disulfide]]
-[[Category: Fatty acid binding protein]]
-[[Category: Mutant]]
-[[Category: Transport protein]]

6l7k

From Proteopedia

Current revision

solution structure of hIFABP V60C/Y70C variant.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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