View source for 1wqj


==Structural Basis for the Regulation of Insulin-Like Growth Factors (IGFs) by IGF Binding Proteins (IGFBPs)==
<StructureSection load='1wqj' size='340' side='right'caption='[[1wqj]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wqj]] is a 2 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=1WQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WQJ 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]] 1.6&#8491;</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=1wqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wqj OCA], [https://pdbe.org/1wqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wqj RCSB], [https://www.ebi.ac.uk/pdbsum/1wqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wqj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IBP4_HUMAN IBP4_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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1wqj ConSurf].
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== Publication Abstract from PubMed ==
Insulin-like growth factor binding proteins (IGFBPs) control the extracellular distribution, function, and activity of IGFs. Here, we report an X-ray structure of the binary complex of IGF-I and the N-terminal domain of IGFBP-4 (NBP-4, residues 3-82) and a model of the ternary complex of IGF-I, NBP-4, and the C-terminal domain (CBP-4, residues 151-232) derived from diffraction data with weak definition of the C-terminal domain. These structures show how the IGFBPs regulate IGF signaling. Key features of the structures include (1) a disulphide bond ladder that binds to IGF and partially masks the IGF residues responsible for type 1 IGF receptor (IGF-IR) binding, (2) the high-affinity IGF-I interaction site formed by residues 39-82 in a globular fold, and (3) CBP-4 interactions. Although CBP-4 does not bind individually to either IGF-I or NBP-4, in the ternary complex, CBP-4 contacts both and also blocks the IGF-IR binding region of IGF-I.

Structural basis for the regulation of insulin-like growth factors by IGF binding proteins.,Siwanowicz I, Popowicz GM, Wisniewska M, Huber R, Kuenkele KP, Lang K, Engh RA, Holak TA Structure. 2005 Jan;13(1):155-67. PMID:15642270<ref>PMID:15642270</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1wqj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Insulin-like growth factor|Insulin-like growth factor]]
*[[Insulin-like growth factor binding protein 3D structures|Insulin-like growth factor binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Engh RA]]
[[Category: Holak TA]]
[[Category: Huber R]]
[[Category: Kuenkele KP]]
[[Category: Lang K]]
[[Category: Popowicz GM]]
[[Category: Siwanowicz I]]
[[Category: Wisniewska M]]