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==C-terminal domain of Insulin-like Growth Factor Binding Protein-1 isolated from human amniotic fluid complexed with Iron(II)== | |||
<StructureSection load='1zt5' size='340' side='right'caption='[[1zt5]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zt5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZT5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.818Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></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=1zt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zt5 OCA], [https://pdbe.org/1zt5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zt5 RCSB], [https://www.ebi.ac.uk/pdbsum/1zt5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zt5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IBP1_HUMAN IBP1_HUMAN] IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration.<ref>PMID:15972819</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zt/1zt5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<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/main_output.php?pdb_ID=1zt5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Insulin-like growth factor (IGF)-binding protein-1 (IGFBP-1) regulates the activity of the insulin-like growth factors in early pregnancy and is, thus, thought to play a key role at the fetal-maternal interface. The C-terminal domain of IGFBP-1 and three isoforms of the intact protein were isolated from human amniotic fluid, and sequencing of the four N-terminal polypeptide chains showed them to be highly pure. The addition of both intact IGFBP-1 and its C-terminal fragment to cultured fibroblasts has a similar stimulating effect on cell migration, and therefore, the domain has a biological activity on its own. The three-dimensional structure of the C-terminal domain was determined by x-ray crystallography to 1.8 Angstroms resolution. The fragment folds as a thyroglobulin type I domain and was found to bind the Fe(2+) ion in the crystals through the only histidine residue present in the polypeptide chain. Iron (II) decreases the binding of intact IGFBP-1 and the C-terminal domain to IGF-II, suggesting that the metal binding site is close to or part of the surface of interaction of the two molecules. | |||
Structure and properties of the C-terminal domain of insulin-like growth factor-binding protein-1 isolated from human amniotic fluid.,Sala A, Capaldi S, Campagnoli M, Faggion B, Labo S, Perduca M, Romano A, Carrizo ME, Valli M, Visai L, Minchiotti L, Galliano M, Monaco HL J Biol Chem. 2005 Aug 19;280(33):29812-9. Epub 2005 Jun 22. PMID:15972819<ref>PMID:15972819</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zt5" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Insulin-like growth factor binding protein 3D structures|Insulin-like growth factor binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Campagnoli | [[Category: Campagnoli M]] | ||
[[Category: Capaldi | [[Category: Capaldi S]] | ||
[[Category: Carrizo | [[Category: Carrizo ME]] | ||
[[Category: Faggion | [[Category: Faggion B]] | ||
[[Category: Galliano | [[Category: Galliano M]] | ||
[[Category: Labo | [[Category: Labo S]] | ||
[[Category: Minchiotti | [[Category: Minchiotti L]] | ||
[[Category: Monaco | [[Category: Monaco HL]] | ||
[[Category: Perduca | [[Category: Perduca M]] | ||
[[Category: Romano | [[Category: Romano A]] | ||
[[Category: Sala | [[Category: Sala A]] | ||
[[Category: Valli | [[Category: Valli M]] | ||
[[Category: Visai | [[Category: Visai L]] | ||
Latest revision as of 11:12, 15 May 2024
C-terminal domain of Insulin-like Growth Factor Binding Protein-1 isolated from human amniotic fluid complexed with Iron(II)C-terminal domain of Insulin-like Growth Factor Binding Protein-1 isolated from human amniotic fluid complexed with Iron(II)
Structural highlights
FunctionIBP1_HUMAN IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration.[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 PubMedInsulin-like growth factor (IGF)-binding protein-1 (IGFBP-1) regulates the activity of the insulin-like growth factors in early pregnancy and is, thus, thought to play a key role at the fetal-maternal interface. The C-terminal domain of IGFBP-1 and three isoforms of the intact protein were isolated from human amniotic fluid, and sequencing of the four N-terminal polypeptide chains showed them to be highly pure. The addition of both intact IGFBP-1 and its C-terminal fragment to cultured fibroblasts has a similar stimulating effect on cell migration, and therefore, the domain has a biological activity on its own. The three-dimensional structure of the C-terminal domain was determined by x-ray crystallography to 1.8 Angstroms resolution. The fragment folds as a thyroglobulin type I domain and was found to bind the Fe(2+) ion in the crystals through the only histidine residue present in the polypeptide chain. Iron (II) decreases the binding of intact IGFBP-1 and the C-terminal domain to IGF-II, suggesting that the metal binding site is close to or part of the surface of interaction of the two molecules. Structure and properties of the C-terminal domain of insulin-like growth factor-binding protein-1 isolated from human amniotic fluid.,Sala A, Capaldi S, Campagnoli M, Faggion B, Labo S, Perduca M, Romano A, Carrizo ME, Valli M, Visai L, Minchiotti L, Galliano M, Monaco HL J Biol Chem. 2005 Aug 19;280(33):29812-9. Epub 2005 Jun 22. PMID:15972819[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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