View source for 1bqt


==THREE-DIMENSIONAL STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR-I (IGF-I) DETERMINED BY 1H-NMR AND DISTANCE GEOMETRY, 6 STRUCTURES==
<StructureSection load='1bqt' size='340' side='right'caption='[[1bqt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bqt]] 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=1BQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 6 models</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=1bqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqt OCA], [https://pdbe.org/1bqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bqt RCSB], [https://www.ebi.ac.uk/pdbsum/1bqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bqt ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/IGF1_HUMAN IGF1_HUMAN] Defects in IGF1 are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) [MIM:[https://omim.org/entry/608747 608747]. IGF1 deficiency is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation.
== Function ==
[https://www.uniprot.org/uniprot/IGF1_HUMAN IGF1_HUMAN] The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake.<ref>PMID:21076856</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/bq/1bqt_consurf.spt"</scriptWhenChecked>
    <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=1bqt ConSurf].
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== Publication Abstract from PubMed ==
The three-dimensional structure of human insulin-like growth factor-I has been determined through a combination of NMR measurements and distance geometry calculations. A total of 320 interatomic distance constraints, including 12 related to the disulfide bridges, were used in these calculations. The resulting structure is characterized by the presence of three helical rods corresponding to the sequence regions, Ala8-Cys18, Gly42-Cys48 and Leu54-Cys61. Furthermore, a turn structure and an extended structure exist in the Gly19-Gly22 and Phe23-Asn26 regions, respectively. Neglecting the N- and C-termini, with their expectedly high degree of mobility as well as a fluctuating C-domain, the r.m.s.d. value is 1.9 A for backbone atoms. Those of the three alpha-helical regions are 1.0, 0.9 and 0.8 A, respectively, 1.8 A being that for the total backbone atoms participating in the formation of these three helices, showing the good convergence of their spatial arrangements. The overall structure obtained here shows that the human IGF-I molecule folds into a spatial structure very similar to that of insulin in an aqueous solution.

Three-dimensional structure of human insulin-like growth factor-I (IGF-I) determined by 1H-NMR and distance geometry.,Sato A, Nishimura S, Ohkubo T, Kyogoku Y, Koyama S, Kobayashi M, Yasuda T, Kobayashi Y Int J Pept Protein Res. 1993 May;41(5):433-40. PMID:8391516<ref>PMID:8391516</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Insulin-like growth factor|Insulin-like growth factor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kobayashi M]]
[[Category: Kobayashi Y]]
[[Category: Koyama S]]
[[Category: Kyogoku Y]]
[[Category: Nishimura S]]
[[Category: Ohkubo T]]
[[Category: Sato A]]
[[Category: Yasuda T]]