Alpha-1-antitrypsin

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<StructureSection load='' size='450' side='right' scene='User:Daniel_Seeman/Alpha-1-antitrypsin/437437437437/1' caption=''>
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<StructureSection load='' size='350' side='right' scene='User:Daniel_Seeman/Alpha-1-antitrypsin/437437437437/1' caption='Transition of α1-antitrypsin between active and inactive conformations '>
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__TOC__
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=== Function ===
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'''Alpha-1-antitrypsin''' (also known as α1-antitrypsin or A1AT) is an inhibitor of [[Elastase]] and [[Trypsin]]. It is a member of the '''Ser'''ine '''P'''rotease '''I'''nhibitor ([[:Category:Serpin|Serpin]]) family, and as such undergoes a conformational change where the substrate protein associates with a loop region on A1AT causing that loop to become ordered as a Beta Strand<ref name="nature_paper">''Nature'' '''455''', 1189-1190 (30 October 2008)</ref>. In this case Trypsin (the substrate) is inhibited when a covalent bond is formed to A1AT through the newly formed Beta region<ref name="nature_paper" />. Once bound covalently to its substrate the stability of the A1AT complex goes up drastically, making it an effective "molecular mousetrap"<ref name="nature_paper" />. With A1AT, as with most members of the Serpin family, the transition from inactive precursor protein to active complex comes after a cleavage event<ref name="nature_paper" />.
'''Alpha-1-antitrypsin''' (also known as α1-antitrypsin or A1AT) is an inhibitor of [[Elastase]] and [[Trypsin]]. It is a member of the '''Ser'''ine '''P'''rotease '''I'''nhibitor ([[:Category:Serpin|Serpin]]) family, and as such undergoes a conformational change where the substrate protein associates with a loop region on A1AT causing that loop to become ordered as a Beta Strand<ref name="nature_paper">''Nature'' '''455''', 1189-1190 (30 October 2008)</ref>. In this case Trypsin (the substrate) is inhibited when a covalent bond is formed to A1AT through the newly formed Beta region<ref name="nature_paper" />. Once bound covalently to its substrate the stability of the A1AT complex goes up drastically, making it an effective "molecular mousetrap"<ref name="nature_paper" />. With A1AT, as with most members of the Serpin family, the transition from inactive precursor protein to active complex comes after a cleavage event<ref name="nature_paper" />.
Shown <scene name='User:Daniel_Seeman/Alpha-1-antitrypsin/437437437437/1'>on the right</scene> is a morph, generated by the <span class="plainlinks">[http://molmovdb.mbb.yale.edu/molmovdb/morph/ Yale Morph Server]</span> that shows A1AT going from its inactive form, to the conformation in which it is bound to Trypsin (also shown in the same animation)<ref>The <span class="plainlinks">[http://molmovdb.mbb.yale.edu/molmovdb/morph/ Yale Morph Server]</span></ref>.
Shown <scene name='User:Daniel_Seeman/Alpha-1-antitrypsin/437437437437/1'>on the right</scene> is a morph, generated by the <span class="plainlinks">[http://molmovdb.mbb.yale.edu/molmovdb/morph/ Yale Morph Server]</span> that shows A1AT going from its inactive form, to the conformation in which it is bound to Trypsin (also shown in the same animation)<ref>The <span class="plainlinks">[http://molmovdb.mbb.yale.edu/molmovdb/morph/ Yale Morph Server]</span></ref>.
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*<scene name='User:Daniel_Seeman/Alpha-1-antitrypsin/A1at_test/1'>A1AT as represented by pdb ID 1atu</scene>
*<scene name='User:Daniel_Seeman/Alpha-1-antitrypsin/A1at_test/1'>A1AT as represented by pdb ID 1atu</scene>
*<scene name='User:Daniel_Seeman/Alpha-1-antitrypsin/A1at_test2/1'>A1AT bound to Trypsin (its substrate)</scene>
*<scene name='User:Daniel_Seeman/Alpha-1-antitrypsin/A1at_test2/1'>A1AT bound to Trypsin (its substrate)</scene>
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</StructureSection>
 
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__NOTOC__
 
==3D structures of Alpha-1-antitrypsin==
==3D structures of Alpha-1-antitrypsin==
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[[Alpha-1-antitrypsin 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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__NOTOC__
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===Uncleaved A1AT===
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[[1qlp]], [[2qug]], [[3cwl]], [[7api]], [[8api]], [[9api]], [[3ne4]] - hA1AT – human<br />
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[[1atu]], [[1psi]], [[1hp7]], [[3dru]], [[3drm]], [[1iz2]], [[1kct]] – hA1AT (mutant)<br />
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[[3t1p]] - hA1AT (mutant) residues 48-418<br />
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[[1ezx]] - hA1AT fragment + trypsin<br />
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[[1oph]] - hA1AT (mutant) + trypsinogen (mutant)<br />
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[[1oo8]] - hA1AT precursor (mutant)<br />
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[[2d26]] - hA1AT + elastase-1<br />
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[[3cwm]] - hA1AT + citrate
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===Cleaved A1AT===
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[[3ndd]], [[3ndf]], [[1qmb]] – hA1AT (mutant)<br />
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Current revision

Transition of α1-antitrypsin between active and inactive conformations

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References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Nature 455, 1189-1190 (30 October 2008)
  2. ↑ The Yale Morph Server
  3. ↑ Biochemistry, Fifth Edition, p.289.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Daniel Seeman, Alexander Berchansky, Joel L. Sussman

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