1hrp: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1hrp.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1hrp", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1hrp|  PDB=1hrp  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN'''


==CRYSTAL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN==
<StructureSection load='1hrp' size='340' side='right'caption='[[1hrp]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hrp]] 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=1HRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRP 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1hrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrp OCA], [https://pdbe.org/1hrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hrp RCSB], [https://www.ebi.ac.uk/pdbsum/1hrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hrp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CGB3_HUMAN CGB3_HUMAN]
== 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/hr/1hrp_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=1hrp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of human chorionic gonadotropin shows that each of its two different subunits has a similar topology, with three disulphide bonds forming a cystine knot. This same folding motif is found in some protein growth factors. The heterodimer is stabilized by a segment of the beta-subunit which wraps around the alpha-subunit and is covalently linked like a seat belt by the disulphide Cys 26-Cys 110. This extraordinary feature appears to be essential not only for the association of these heterodimers but also for receptor binding by the glycoprotein hormones.


==Overview==
Crystal structure of human chorionic gonadotropin.,Lapthorn AJ, Harris DC, Littlejohn A, Lustbader JW, Canfield RE, Machin KJ, Morgan FJ, Isaacs NW Nature. 1994 Jun 9;369(6480):455-61. PMID:8202136<ref>PMID:8202136</ref>
The three-dimensional structure of human chorionic gonadotropin shows that each of its two different subunits has a similar topology, with three disulphide bonds forming a cystine knot. This same folding motif is found in some protein growth factors. The heterodimer is stabilized by a segment of the beta-subunit which wraps around the alpha-subunit and is covalently linked like a seat belt by the disulphide Cys 26-Cys 110. This extraordinary feature appears to be essential not only for the association of these heterodimers but also for receptor binding by the glycoprotein hormones.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1HRP is a [[Protein complex]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRP OCA].
</div>
<div class="pdbe-citations 1hrp" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of human chorionic gonadotropin., Lapthorn AJ, Harris DC, Littlejohn A, Lustbader JW, Canfield RE, Machin KJ, Morgan FJ, Isaacs NW, Nature. 1994 Jun 9;369(6480):455-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8202136 8202136]
*[[Hormone|Hormone]]
[[Category: Protein complex]]
*[[Human Follicle-Stimulating Hormone Complexed with its Receptor|Human Follicle-Stimulating Hormone Complexed with its Receptor]]
[[Category: Harris, D C.]]
== References ==
[[Category: Isaacs, N W.]]
<references/>
[[Category: Lapthorn, A J.]]
__TOC__
[[Category: Hormone]]
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:10:03 2008''
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Harris DC]]
[[Category: Isaacs NW]]
[[Category: Lapthorn AJ]]
Retrieved from "https://proteopedia.org/1hrp"