3t1p
From Proteopedia
(Difference between revisions)
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<StructureSection load='3t1p' size='340' side='right' caption='[[3t1p]], [[Resolution|resolution]] 3.90Å' scene=''> | <StructureSection load='3t1p' size='340' side='right' caption='[[3t1p]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3t1p]] is a 1 chain structure | + | <table><tr><td colspan='2'>[[3t1p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T1P FirstGlance]. <br> |
| - | </td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1p OCA], [http://pdbe.org/3t1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t1p RCSB], [http://www.ebi.ac.uk/pdbsum/3t1p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1p ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1p OCA], [http://pdbe.org/3t1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t1p RCSB], [http://www.ebi.ac.uk/pdbsum/3t1p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1p ProSAT]</span></td></tr> | + | |
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> | [[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | alpha(1)-Antitrypsin (alpha1AT) deficiency is a disease with multiple manifestations, including cirrhosis and emphysema, caused by the accumulation of stable polymers of mutant protein in the endoplasmic reticulum of hepatocytes. However, the molecular basis of misfolding and polymerization remain unknown. We produced and crystallized a trimeric form of alpha1AT that is recognized by an antibody specific for the pathological polymer. Unexpectedly, this structure reveals a polymeric linkage mediated by domain swapping the carboxy-terminal 34 residues. Disulphide-trapping and antibody-binding studies further demonstrate that runaway C-terminal domain swapping, rather than the s4A/s5A domain swap previously proposed, underlies polymerization of the common Z-mutant of alpha1AT in vivo. | ||
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| + | Molecular basis of alpha1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer.,Yamasaki M, Sendall TJ, Pearce MC, Whisstock JC, Huntington JA EMBO Rep. 2011 Sep 30;12(10):1011-7. doi: 10.1038/embor.2011.171. PMID:21909074<ref>PMID:21909074</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3t1p" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Human]] | ||
[[Category: Huntington, J A]] | [[Category: Huntington, J A]] | ||
[[Category: Yamasaki, M]] | [[Category: Yamasaki, M]] | ||
Revision as of 11:46, 3 August 2017
Crystal structure of an alpha-1-antitrypsin trimer
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