Structural aspects of serpin inhibition
The essential roles of proteins of the serpin family in many physiological processes, along with new discoveries of their unique folding properties, have attracted intense interest in recent years. Many serpins display unusual mobile behavior attributed to rearrangements of α-helical or β-sheet doma...
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Veröffentlicht in: | FEBS Letters 1994-05, Vol.344 (2), p.117-124 |
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creator | Schulze, Andreas J. Huber, Robert Bode, Wolfram Engh, Richard A. |
description | The essential roles of proteins of the serpin family in many physiological processes, along with new discoveries of their unique folding properties, have attracted intense interest in recent years. Many serpins display unusual mobile behavior attributed to rearrangements of α-helical or β-sheet domains, whereby large scale transitions accompany a variety of functions, including inactivation. This unusual behavior was first recognized with the X-ray structure of modified α1-proteinase inhibitor. Subsequent experiments, including new X-ray structures, have revealed a surprising variety of conformations which are functionally important but only partially understood. We review here experimental evidence for conformations relevant to the serpin inhibitory mechanism. |
doi_str_mv | 10.1016/0014-5793(94)00369-6 |
format | Article |
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Many serpins display unusual mobile behavior attributed to rearrangements of α-helical or β-sheet domains, whereby large scale transitions accompany a variety of functions, including inactivation. This unusual behavior was first recognized with the X-ray structure of modified α1-proteinase inhibitor. Subsequent experiments, including new X-ray structures, have revealed a surprising variety of conformations which are functionally important but only partially understood. We review here experimental evidence for conformations relevant to the serpin inhibitory mechanism.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Canonical conformation</subject><subject>Crystalline structure</subject><subject>Crystallography, X-Ray</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Models, Molecular</subject><subject>Molecular biophysics</subject><subject>Molecular Structure</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Serpin</subject><subject>Serpins - chemistry</subject><subject>Structural transition</subject><subject>Structure in molecular biology</subject><subject>X-ray structure</subject><subject>β-sheet</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1LxDAQhoMo67r6DxR6ED8O1aRJ0-Yi6LKrwoIH9RzSdIqRbluTVtl_b7otexQPIWTmmXdm3iB0SvANwYTfYkxYGCeCXgl2jTHlIuR7aErShIaU8XQfTXfIITpy7hP7d0rEBE1ST6VcTNHla2s73XZWlYFyDejWBXUROLCNqQJTfZjMtKaujtFBoUoHJ-M9Q-_Lxdv8KVy9PD7P71ehZkzwkPgWAIRkOM2iXBPGcqqBxqCzjCumkzgTWLEi0kphkTJ_Ep5RSETEU8UVnaGLQbex9VcHrpVr4zSUpaqg7pxMOBM0jrAH2QBqWztnoZCNNWtlN5Jg2fsj--Vlv7wUTG79kdyXnY36XbaGfFc0GuLz52NeOa3KwqpKG7fDGCFciNhjywH7MSVs_tVaLhcPUZ_o44Jto_08d4MQeFO_DVjptIFKQ26s_wyZ1-bvhX4BedeTCA</recordid><startdate>19940516</startdate><enddate>19940516</enddate><creator>Schulze, Andreas J.</creator><creator>Huber, Robert</creator><creator>Bode, Wolfram</creator><creator>Engh, Richard A.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19940516</creationdate><title>Structural aspects of serpin inhibition</title><author>Schulze, Andreas J. ; Huber, Robert ; Bode, Wolfram ; Engh, Richard A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4496-1000ee11b08b2dc144d3ce35ecbb6a4c75b90a4f2caa098409876b3e79268a6a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Canonical conformation</topic><topic>Crystalline structure</topic><topic>Crystallography, X-Ray</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Models, Molecular</topic><topic>Molecular biophysics</topic><topic>Molecular Structure</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Serpin</topic><topic>Serpins - chemistry</topic><topic>Structural transition</topic><topic>Structure in molecular biology</topic><topic>X-ray structure</topic><topic>β-sheet</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schulze, Andreas J.</creatorcontrib><creatorcontrib>Huber, Robert</creatorcontrib><creatorcontrib>Bode, Wolfram</creatorcontrib><creatorcontrib>Engh, Richard A.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS Letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schulze, Andreas J.</au><au>Huber, Robert</au><au>Bode, Wolfram</au><au>Engh, Richard A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural aspects of serpin inhibition</atitle><jtitle>FEBS Letters</jtitle><addtitle>FEBS Lett</addtitle><date>1994-05-16</date><risdate>1994</risdate><volume>344</volume><issue>2</issue><spage>117</spage><epage>124</epage><pages>117-124</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>The essential roles of proteins of the serpin family in many physiological processes, along with new discoveries of their unique folding properties, have attracted intense interest in recent years. 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subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Canonical conformation Crystalline structure Crystallography, X-Ray Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrolases Models, Molecular Molecular biophysics Molecular Structure Protein Conformation Protein Structure, Secondary Serpin Serpins - chemistry Structural transition Structure in molecular biology X-ray structure β-sheet |
title | Structural aspects of serpin inhibition |
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