Interhelical hydrogen bonding drives strong interactions in membrane proteins
Polar residues in transmembrane α-helices may strongly influence the folding or association of integral membrane proteins. To test whether a motif that promotes helix association in a soluble protein could do the same within a membrane, we designed a model transmembrane helix based on the GCN4 leuci...
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| Veröffentlicht in: | Nature Structural Biology 2000-02, Vol.7 (2), p.154-160 |
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| container_title | Nature Structural Biology |
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| creator | Xiao Zhou, Fang Cocco, Melanie J. Russ, William P. Brunger, Axel T. Engelman, Donald M. |
| description | Polar residues in transmembrane α-helices may strongly influence the folding or association of integral membrane proteins. To test whether a motif that promotes helix association in a soluble protein could do the same within a membrane, we designed a model transmembrane helix based on the GCN4 leucine zipper. We found in both detergent miscelles and biological membranes that helix association is driven strongly by asparagine, independent of the rest of the hydrophobic leucine and/or valine sequence. Hydrogen bonding between membrane helices gives stronger associations than the packing of surfaces in glycophorin A helices, creating an opportunity to stabilize structures, but also implying a danger that non-specific interactions might occur. Thus, membrane proteins may fold to avoid exposure of strongly hydrogen bonding groups at their lipid exposed surfaces. |
| doi_str_mv | 10.1038/72430 |
| format | Article |
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To test whether a motif that promotes helix association in a soluble protein could do the same within a membrane, we designed a model transmembrane helix based on the GCN4 leucine zipper. We found in both detergent miscelles and biological membranes that helix association is driven strongly by asparagine, independent of the rest of the hydrophobic leucine and/or valine sequence. Hydrogen bonding between membrane helices gives stronger associations than the packing of surfaces in glycophorin A helices, creating an opportunity to stabilize structures, but also implying a danger that non-specific interactions might occur. Thus, membrane proteins may fold to avoid exposure of strongly hydrogen bonding groups at their lipid exposed surfaces.</description><identifier>ISSN: 1072-8368</identifier><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/72430</identifier><identifier>PMID: 10655619</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Asparagine - chemistry ; Biochemistry ; Biological membranes ; Biological Microscopy ; Biomedical and Life Sciences ; Cell Membrane - metabolism ; Chloramphenicol O-Acetyltransferase - chemistry ; Chloramphenicol O-Acetyltransferase - genetics ; Chloramphenicol O-Acetyltransferase - metabolism ; Circular Dichroism ; Detergents - chemistry ; Dimerization ; DNA-Binding Proteins ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins - chemistry ; Glycophorin - chemistry ; Glycophorin - genetics ; Glycophorin - metabolism ; Hydrogen ; Hydrogen Bonding ; Leucine Zippers ; Life Sciences ; Magnetic Resonance Spectroscopy ; Membrane Biology ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Micelles ; Micrococcal Nuclease - chemistry ; Molecular Sequence Data ; Peptides - chemistry ; Protein Conformation ; Protein Kinases - chemistry ; Protein Structure ; Protein Structure, Secondary ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Saccharomyces cerevisiae Proteins</subject><ispartof>Nature Structural Biology, 2000-02, Vol.7 (2), p.154-160</ispartof><rights>Nature America Inc. 2000</rights><rights>Copyright Nature Publishing Group Feb 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/72430$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/72430$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10655619$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xiao Zhou, Fang</creatorcontrib><creatorcontrib>Cocco, Melanie J.</creatorcontrib><creatorcontrib>Russ, William P.</creatorcontrib><creatorcontrib>Brunger, Axel T.</creatorcontrib><creatorcontrib>Engelman, Donald M.</creatorcontrib><title>Interhelical hydrogen bonding drives strong interactions in membrane proteins</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Biol</addtitle><description>Polar residues in transmembrane α-helices may strongly influence the folding or association of integral membrane proteins. To test whether a motif that promotes helix association in a soluble protein could do the same within a membrane, we designed a model transmembrane helix based on the GCN4 leucine zipper. We found in both detergent miscelles and biological membranes that helix association is driven strongly by asparagine, independent of the rest of the hydrophobic leucine and/or valine sequence. Hydrogen bonding between membrane helices gives stronger associations than the packing of surfaces in glycophorin A helices, creating an opportunity to stabilize structures, but also implying a danger that non-specific interactions might occur. Thus, membrane proteins may fold to avoid exposure of strongly hydrogen bonding groups at their lipid exposed surfaces.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Asparagine - chemistry</subject><subject>Biochemistry</subject><subject>Biological membranes</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Chloramphenicol O-Acetyltransferase - chemistry</subject><subject>Chloramphenicol O-Acetyltransferase - genetics</subject><subject>Chloramphenicol O-Acetyltransferase - metabolism</subject><subject>Circular Dichroism</subject><subject>Detergents - chemistry</subject><subject>Dimerization</subject><subject>DNA-Binding Proteins</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fungal Proteins - chemistry</subject><subject>Glycophorin - chemistry</subject><subject>Glycophorin - genetics</subject><subject>Glycophorin - metabolism</subject><subject>Hydrogen</subject><subject>Hydrogen Bonding</subject><subject>Leucine Zippers</subject><subject>Life Sciences</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Membrane Biology</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Micelles</subject><subject>Micrococcal Nuclease - chemistry</subject><subject>Molecular Sequence Data</subject><subject>Peptides - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Kinases - chemistry</subject><subject>Protein Structure</subject><subject>Protein Structure, Secondary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><issn>1072-8368</issn><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkElPwzAQhS0EoqX0L6CIA7eAx0tsH1HFUqmIC5yjLJPWVeIUO0Hqv8dlUSVOM6P59N7TI2QO9BYo13eKCU5PyBSkkKkxWp7GnSqWap7pCbkIYUspk1LxczIBmkmZgZmSl6Ub0G-wtVXRJpt97fs1uqTsXW3dOqm9_cSQhMH38bIHtqgG27sQj6TDrvSFw2Tn-wGtC5fkrCnagPPfOSPvjw9vi-d09fq0XNyv0h3L5JCqAqBhqARIwzNTCckh41XNmkoh1oASSiiUkRUVEo2SKmtYozSgqAWjwGfk5kc3Gn-MGIa8s6HCto1h-jHkimptJFURvP4HbvvRu5gtZ0wzbQTwCF39QmPZYZ3vvO0Kv8__Wjrahfhya_RHFaD5of78u37-BUEmczs</recordid><startdate>20000201</startdate><enddate>20000201</enddate><creator>Xiao Zhou, Fang</creator><creator>Cocco, Melanie J.</creator><creator>Russ, William P.</creator><creator>Brunger, Axel T.</creator><creator>Engelman, Donald M.</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20000201</creationdate><title>Interhelical hydrogen bonding drives strong interactions in membrane proteins</title><author>Xiao Zhou, Fang ; Cocco, Melanie J. ; Russ, William P. ; Brunger, Axel T. ; Engelman, Donald M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p265t-7a11f2e74159369c453163cd2fc7eed1e51b1a795c045e97576f2f781e4d42013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Asparagine - 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Academic</collection><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xiao Zhou, Fang</au><au>Cocco, Melanie J.</au><au>Russ, William P.</au><au>Brunger, Axel T.</au><au>Engelman, Donald M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interhelical hydrogen bonding drives strong interactions in membrane proteins</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>2000-02-01</date><risdate>2000</risdate><volume>7</volume><issue>2</issue><spage>154</spage><epage>160</epage><pages>154-160</pages><issn>1072-8368</issn><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Polar residues in transmembrane α-helices may strongly influence the folding or association of integral membrane proteins. To test whether a motif that promotes helix association in a soluble protein could do the same within a membrane, we designed a model transmembrane helix based on the GCN4 leucine zipper. We found in both detergent miscelles and biological membranes that helix association is driven strongly by asparagine, independent of the rest of the hydrophobic leucine and/or valine sequence. Hydrogen bonding between membrane helices gives stronger associations than the packing of surfaces in glycophorin A helices, creating an opportunity to stabilize structures, but also implying a danger that non-specific interactions might occur. Thus, membrane proteins may fold to avoid exposure of strongly hydrogen bonding groups at their lipid exposed surfaces.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>10655619</pmid><doi>10.1038/72430</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Motifs Amino Acid Sequence Asparagine - chemistry Biochemistry Biological membranes Biological Microscopy Biomedical and Life Sciences Cell Membrane - metabolism Chloramphenicol O-Acetyltransferase - chemistry Chloramphenicol O-Acetyltransferase - genetics Chloramphenicol O-Acetyltransferase - metabolism Circular Dichroism Detergents - chemistry Dimerization DNA-Binding Proteins Electrophoresis, Polyacrylamide Gel Fungal Proteins - chemistry Glycophorin - chemistry Glycophorin - genetics Glycophorin - metabolism Hydrogen Hydrogen Bonding Leucine Zippers Life Sciences Magnetic Resonance Spectroscopy Membrane Biology Membrane Proteins - chemistry Membrane Proteins - metabolism Micelles Micrococcal Nuclease - chemistry Molecular Sequence Data Peptides - chemistry Protein Conformation Protein Kinases - chemistry Protein Structure Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Saccharomyces cerevisiae Proteins |
| title | Interhelical hydrogen bonding drives strong interactions in membrane proteins |
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