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1dip

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Revision as of 11:07, 28 July 2021

THE SOLUTION STRUCTURE OF PORCINE DELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE, NMR, 10 STRUCTURES

Structural highlights

1dip is a 2 chain structure with sequence from Pig. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[T22D3_PIG] Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The 77-residue delta sleep-inducing peptide immunoreactive peptide (DIP) is a close homolog of the Drosophila melanogaster shortsighted gene product. Porcine DIP (pDIP) and a peptide containing a leucine zipper-related partial sequence of pDIP, pDIP(9-46), was synthesized and studied by circular dichroism and nuclear magnetic resonance spectroscopy in combination with molecular dynamics calculations. Ultracentrifugation, size exclusion chromatography, and model calculations indicated that pDIP forms a dimer. This was confirmed by the observation of concentration-dependent thermal folding-unfolding transitions. From CD spectroscopy and thermal folding-unfolding transitions of pDIP(9-46), it was concluded that the dimerization of pDIP is a result of interaction between helical structures localized in the leucine zipper motif. The three-dimensional structure of the protein was determined with a modified simulated annealing protocol using experimental data derived from nuclear magnetic resonance spectra and a modeling approach based on an established strategy for coiled coil structures. The left-handed super helical structure of the leucine zipper type sequence resulting from the modeling approach is in agreement with known leucine zipper structures. In addition to the hydrophobic interactions between the amino acids at the heptade positions a and d, the structure of pDIP is stabilized by the formation of interhelical i to i' + 5 salt bridges. This result was confirmed by the pH dependence of the thermal-folding transitions. In addition to the amphipatic helix of the leucine zipper, a second helix is formed in the NH2-terminal part of pDIP. This helix exhibits more 310-helix character and is less stable than the leucine zipper helix. For the COOH-terminal region of pDIP no elements of regular secondary structure were observed.

Solution structure of porcine delta sleep-inducing peptide immunoreactive peptide A homolog of the shortsighted gene product.,Seidel G, Adermann K, Schindler T, Ejchart A, Jaenicke R, Forssmann WG, Rosch P J Biol Chem. 1997 Dec 5;272(49):30918-27. PMID:9388238^[1]

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

References

↑ Seidel G, Adermann K, Schindler T, Ejchart A, Jaenicke R, Forssmann WG, Rosch P. Solution structure of porcine delta sleep-inducing peptide immunoreactive peptide A homolog of the shortsighted gene product. J Biol Chem. 1997 Dec 5;272(49):30918-27. PMID:9388238

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dip"

@@ Line 3: / Line 3: @@
 <StructureSection load='1dip' size='340' side='right'caption='[[1dip]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dip]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DIP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dip]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DIP FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dip OCA], [http://pdbe.org/1dip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dip RCSB], [http://www.ebi.ac.uk/pdbsum/1dip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dip 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=1dip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dip OCA], [https://pdbe.org/1dip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dip RCSB], [https://www.ebi.ac.uk/pdbsum/1dip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dip ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/T22D3_PIG T22D3_PIG]] Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities (By similarity).
+[[https://www.uniprot.org/uniprot/T22D3_PIG T22D3_PIG]] Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1dip

From Proteopedia

Revision as of 11:07, 28 July 2021

THE SOLUTION STRUCTURE OF PORCINE DELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE, NMR, 10 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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