← all pages
2.12:_Glycoproteins
view live ↗
<p class="lt-bio-3790" style="background-color: unset;">Glycoproteins have carbohydrate attached to them — a process called <strong>glycosylation</strong>. The attachment is a covalent linkage to:</p> <ul> <li class="lt-bio-3790" style="background-color: unset;">the hydroxyl (-OH) group of the R group of serine or threonine - called "<strong>O-linked</strong>" in both cases or to</li> <li class="lt-bio-3790" style="background-color: unset;">the amino group (-NH<sub><font size="2">2</font></sub>) in the R group of asparagine - called "<strong>N-linked</strong>"</li> </ul> <p class="lt-bio-3790" style="background-color: unset;">The carbohydrate consists of short, usually branched, chains of</p> <ul> <li class="lt-bio-3790" style="background-color: unset;">plain sugars (e.g., glucose, galactose)</li> <li class="lt-bio-3790" style="background-color: unset;">amino sugars (sugars with an amino group, e.g., N-acetylglucosamine), and</li> <li class="lt-bio-3790" style="background-color: unset;">acidic sugars (sugars with a carboxyl group, e.g., sialic acid)</li> </ul> <p class="lt-bio-3790" style="background-color: unset;">Sugars are very hydrophilic thanks to their many -OH groups. Their presence</p> <ul> <li class="lt-bio-3790" style="background-color: unset;">makes glycoproteins far more hydrophilic than they would be otherwise and</li> <li class="lt-bio-3790" style="background-color: unset;">are often essential for the proper folding of the protein into its tertiary structure</li> </ul> <p class="lt-bio-3790" style="background-color: unset;">Most of the proteins exposed to the watery surroundings at the surface of cells are glycoproteins.</p> <p class="lt-bio-3790" style="background-color: unset;"><img class="internal right" style="width: 325px; height: 350px; float: right;" alt="Glycophorin spans a lipid bilayer, with carbohydrate chains attached to its extracellular region." loading="lazy" width="325px" height="350px" src="https://bio.libretexts.org/@api/deki/files/5158/glycophorin.gif?revision=1&size=bestfit&width=325&height=350" aria-describedby="remedy-description-30dae56b3695ea0a" /><span id="remedy-description-30dae56b3695ea0a" data-remedy-image-description="30dae56b3695ea0a" style="display: block; white-space: pre-line;">A chain of labeled amino-acid circles runs from the N-terminal end outside the cell, through the lipid bilayer, to the C-terminal end inside. Residue numbers mark positions along the chain. The key identifies blue O-linked carbohydrate symbols attached to orange Ser or Thr residues, and green N-linked carbohydrate attached to a dark blue Asn residue. These carbohydrate attachments occur on the outside portion; the membrane-spanning and inside portions have none shown. The bilayer is drawn as two rows of heads with tails facing inward.</span>This image shows the primary structure of <strong>glycophorin A</strong>, a glycoprotein that spans the plasma membrane ("Lipid bilayer") of human red blood cells. Each RBC has some 500,000 copies of the molecule embedded in its plasma membrane.</p> <ul> <li class="lt-bio-3790" style="background-color: unset;">Fifteen carbohydrate chains are "O-linked" to serine (Ser) and threonine (Thr) residues</li> <li class="lt-bio-3790" style="background-color: unset;">One carbohydrate chain is "N-linked" to the asparagine (Asn) at position 26</li> </ul> <p class="lt-bio-3790" style="background-color: unset;">Two polymorphic versions of glycophorin A, which differ only at residues 1 and 5, occur in humans. These give rise to the MN blood groups</p> <ul> <li class="lt-bio-3790" style="background-color: unset;">The M allele encodes Ser at position 1 (Ser-1) and Gly at position 5 (Gly-5)</li> <li class="lt-bio-3790" style="background-color: unset;">The N allele encodes Leu-1 and Glu-5</li> </ul> <span id="Genotype_to_Phenotype"></span><span id="Genotype_to_Phenotype-2"></span><h2 style="background-color: unset;" class="lt-bio-3790">Genotype to Phenotype</h2> <p class="lt-bio-3790" style="background-color: unset;">Individuals who inherit two N alleles (are homozygous) have blood group N.</p> <ul> <li class="lt-bio-3790" style="background-color: unset;">Individuals who are homozygous for the M allele have blood group M.</li> <li class="lt-bio-3790" style="background-color: unset;">Heterozygous individuals produce both proteins and have blood group <strong>MN</strong>.</li> </ul> <p class="lt-bio-3790" style="background-color: unset;">Glycophorin A is the most important attachment site by which the parasite <em>Plasmodium falciparum</em> invades human red blood cells.</p> <footer class="mt-content-footer"> <style>/*<![CDATA[*/#mt-toc-container {display: none !important;}/*]]>*/</style><script type="text/javascript">/*<![CDATA[*/ $(function() { if(!window['autoDefinitionList']){ window['autoDefinitionList'] = true; $('dl').find('dt').on('click', function() { $(this).next().toggle('350'); }); } });/*]]>*/</script> <script defer="true" src="https://static.cloudflareinsights.com/beacon.min.js" data-cf-beacon="{"token": "483ec2414e274209a7e93c253192df0b"}"></script><script src="https://cdn.libretexts.net/github/LibreTextsMain/Miscellaneous/h5p-resizer.js"></script><script src="https://cdnjs.cloudflare.com/ajax/libs/iframe-resizer/4.2.11/iframeResizer.contentWindow.min.js" integrity="sha512-FOf4suFgz7OrWmBiyyWW48u/+6GaaAFSDHagh2EBu/GH/1+OQSYc0NFGeGeZK0gZ3vuU1ovmzVzD6bxmT4vayg==" crossorigin="anonymous"></script><script src="https://cdnjs.cloudflare.com/ajax/libs/iframe-resizer/4.2.11/iframeResizer.min.js" integrity="sha512-HY1lApSG7xxx8mYzs/lxRs+c5AaDThRaa3pvQB6puiswvf2lWqMJVf+8qSGiL4ZXfHQoPIqbd1TlpqfycPo3cQ==" crossorigin="anonymous"></script><script>/*<![CDATA[*/window.addEventListener('load', function(){$('iframe').iFrameResize({warningTimeout:0, scrolling: 'omit'});})/*]]>*/</script><script>/*<![CDATA[*/ window.PageNum = "auto"; window.InitialOffset = "false"; window.PageName = "2.12: Glycoproteins"; /*]]>*/</script> <hr class="autoattribution-divider" /><div class="autoattribution"><p>This page titled <a target="_blank" class="internal mt-self-link" href="/Sandboxes/johnnyphung/biology/02:_The_Molecules_of_Life/2.12:_Glycoproteins">2.12: Glycoproteins</a> is shared under a <a rel="nofollow" href="https://creativecommons.org/licenses/by/3.0" target="_blank">CC BY 3.0 (creativecommons.org)</a> license and was authored, remixed, and/or curated by <a rel="nofollow" target="_blank" href="http://www.biology-pages.info/">John W. Kimball (biology-pages.info)</a> via <a rel="nofollow" href="https://www.biology-pages.info/" target="_blank">source content (biology-pages.info)</a> that was edited to the style and standards of the LibreTexts platform.</p></div> <script type="text/javascript">/*<![CDATA[*/ try { const pageTagsHolder = document.getElementById('pageTagsHolder'); if (pageTagsHolder) { const pageTagsRaw = pageTagsHolder.innerText; if (pageTagsRaw.includes('transcluded:yes')) { const attrSections = document.querySelectorAll('.autoattribution'); const attrDividers = document.querySelectorAll('.autoattribution-divider'); if (attrSections.length > 1 && attrDividers.length > 1) { /* Hide first AutoAttribution from transcluded page */ attrSections[0].style.display = 'none'; attrDividers[0].style.display = 'none'; } } } } catch (e) { console.error('[AutoAttribution Transclusion Removal] Error encountered!'); console.error(e); }/*]]>*/</script> <div id="librelens-attribution-list"></div></footer>
💾 Save to sandbox
Reset