1tp0

From Proteopedia

(Difference between revisions)

Revision as of 07:03, 5 April 2017

Triple mutation in interleukin 1 beta cavity:replacement of phenylalanines with tryptophan.

Structural highlights

1tp0 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1s0l, 1t4q, 1too, 1twe, 1twm
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[IL1B_HUMAN] Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.^[1]

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 structural and energetic consequences of modifications to the hydrophobic cavity of interleukin 1-beta (IL-1beta) are described. Previous reports demonstrated that the entirely hydrophobic cavity of IL-1beta contains positionally disordered water. To gain a better understanding of the nature of this cavity and the water therein, a number of mutant proteins were constructed by site-directed mutagenesis, designed to result in altered hydrophobicity of the cavity. These mutations involve the replacement of specific phenylalanine residues, which circumscribe the cavity, with tyrosine, tryptophan, leucine and isoleucine. Using differential scanning calorimetry to determine the relative stabilities of the wild-type and mutant proteins, we found all of the mutants to be destabilizing. X-ray crystallography was used to identify the structural consequences of the mutations. No clear correlation between the hydrophobicities of the specific side-chains introduced and the resulting stabilities was found.

Structural and energetic consequences of mutations in a solvated hydrophobic cavity.,Adamek DH, Guerrero L, Blaber M, Caspar DL J Mol Biol. 2005 Feb 11;346(1):307-18. Epub 2004 Dec 24. PMID:15663946^[2]

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

References

↑ Van Damme J, De Ley M, Opdenakker G, Billiau A, De Somer P, Van Beeumen J. Homogeneous interferon-inducing 22K factor is related to endogenous pyrogen and interleukin-1. Nature. 1985 Mar 21-27;314(6008):266-8. PMID:3920526
↑ Adamek DH, Guerrero L, Blaber M, Caspar DL. Structural and energetic consequences of mutations in a solvated hydrophobic cavity. J Mol Biol. 2005 Feb 11;346(1):307-18. Epub 2004 Dec 24. PMID:15663946 doi:10.1016/j.jmb.2004.11.046

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tp0"

@@ Line 1: / Line 1: @@
 ==Triple mutation in interleukin 1 beta cavity:replacement of phenylalanines with tryptophan.==
 <StructureSection load='1tp0' size='340' side='right' caption='[[1tp0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tp0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TP0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tp0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TP0 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s0l|1s0l]], [[1t4q|1t4q]], [[1too|1too]], [[1twe|1twe]], [[1twm|1twm]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1tp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tp0 OCA], [http://pdbe.org/1tp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tp0 RCSB], [http://www.ebi.ac.uk/pdbsum/1tp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tp0 ProSAT]</span></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=1tp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tp0 OCA], [http://pdbe.org/1tp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tp0 RCSB], [http://www.ebi.ac.uk/pdbsum/1tp0 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tp0 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
 [[Category: Adamek, D H]]
 [[Category: Caspar, D L]]

1tp0

From Proteopedia

Revision as of 07:03, 5 April 2017

Triple mutation in interleukin 1 beta cavity:replacement of phenylalanines with tryptophan.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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