1mtp

<table><tr><td colspan='2'>[[1mtp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MTP FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mtp OCA], [https://pdbe.org/1mtp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mtp RCSB], [https://www.ebi.ac.uk/pdbsum/1mtp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mtp ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Serpins utilize conformational change to inhibit target proteinases; the price paid for this conformational flexibility is that many undergo temperature-induced polymerization. Despite this thermolability, serpins are present in the genomes of thermophilic prokaryotes, and here we characterize the first such serpin, thermopin. Thermopin is a proteinase inhibitor and, in comparison with human alpha(1)-antitrypsin, possesses enhanced stability at 60 degrees C. The 1.5 A crystal structure reveals novel structural features in regions implicated in serpin folding and stability. Thermopin possesses a C-terminal "tail" that interacts with the top of the A beta sheet and plays an important role in the folding/unfolding of the molecule. These data provide evidence as to how this unusual serpin has adapted to fold and function in a heated environment.

The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment.,Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC Structure. 2003 Apr;11(4):387-97. PMID:12679017<ref>PMID:12679017</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Thermonospora fusca henssen 1957]]

[[Category: Bottomley, S P]]

[[Category: Cabrita, L D]]

[[Category: Irving, J A]]

[[Category: Pike, R N]]

[[Category: Rossjohn, J]]

[[Category: Whisstock, J C]]

[[Category: Protease inhibitor]]

[[Category: Structural genomic]]