1hcn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1hcn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hcn, resolution 2.6&Aring;" /> '''STRUCTURE OF HUMAN C...)
Current revision (11:30, 27 March 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hcn.gif|left|200px]]<br />
 
-
<applet load="1hcn" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1hcn, resolution 2.6&Aring;" />
 
-
'''STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN'''<br />
 
-
==Overview==
+
==STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN==
-
BACKGROUND: Human chorionic gonadotropin (hCG) is a placental hormone that, stimulates secretion of the pregnancy-sustaining steroid progesterone. It, is a member of a family of glycoprotein hormones that are disulfide-rich, heterodimers, with a common alpha-chain and distinctive beta-chains, specific to their particular G-protein linked receptors. RESULTS: We have, produced recombinant hCG in mammalian cells as the selenomethionyl, protein, and have determined its structure (after partial deglycosylation), at 2.6 A resolution from multiwavelength anomalous diffraction (MAD), measurements. Despite only limited sequence similarity (10% identity), the, alpha- and beta-subunits of hCG have similar tertiary folds. Each subunit, has a cystine-knot motif at its core of extended hairpin loops. There is a, very extensive subunit interface featuring two inter-chain beta-sheets and, a unique, disulfide-tethered 'arm' from the beta-subunit which 'embraces', the alpha-subunit. The carboxy-terminal peptide of the beta-subunit, which, is rich in O-linked sugars, is disordered. CONCLUSIONS: Structural and, sequence comparisons indicate an evolutionary homology, albeit remote, between the glycoprotein hormone chains and other cystine-knot proteins, notably platelet-derived growth factor. Segments of the alpha- and, beta-chains that have been convincingly implicated in receptor binding by, hCG are juxtaposed on one side of the molecule. A glycosylation site, implicated in signal transduction but not in binding is also close to the, presumed binding site suggesting a possible coupling between ligand, binding and signaling. This study with selenomethionyl protein produced in, mammalian cells extends the realm of MAD phasing.
+
<StructureSection load='1hcn' size='340' side='right'caption='[[1hcn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1hcn]] 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=1HCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCN 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]] 2.6&#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=1hcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcn OCA], [https://pdbe.org/1hcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hcn RCSB], [https://www.ebi.ac.uk/pdbsum/1hcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hcn ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GLHA_HUMAN GLHA_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/hc/1hcn_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=1hcn ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1HCN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HCN OCA].
+
*[[Hormone|Hormone]]
-
 
+
*[[Human Follicle-Stimulating Hormone Complexed with its Receptor|Human Follicle-Stimulating Hormone Complexed with its Receptor]]
-
==Reference==
+
__TOC__
-
Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein., Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA, Structure. 1994 Jun 15;2(6):545-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7922031 7922031]
+
</StructureSection>
-
[[Category: Protein complex]]
+
[[Category: Homo sapiens]]
-
[[Category: Canfield, R.E.]]
+
[[Category: Large Structures]]
-
[[Category: Hendrickson, W.A.]]
+
[[Category: Canfield RE]]
-
[[Category: Liu, Y.]]
+
[[Category: Hendrickson WA]]
-
[[Category: Lustbader, J.W.]]
+
[[Category: Liu Y]]
-
[[Category: Wu, H.]]
+
[[Category: Lustbader JW]]
-
[[Category: NAG]]
+
[[Category: Wu H]]
-
[[Category: hormone]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:15:54 2007''
+

Current revision

STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN

PDB ID 1hcn

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hcn"
Personal tools