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| {{STRUCTURE_2pef| PDB=2pef | SCENE= }} | | {{STRUCTURE_2pef| PDB=2pef | SCENE= }} |
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| '''Crystal Structure of a Thermophilic Serpin, Tengpin, in the Latent State'''
| | ===Crystal Structure of a Thermophilic Serpin, Tengpin, in the Latent State=== |
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| ==Overview==
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| Serpins fold to a metastable native state and are susceptible to undergoing spontaneous conformational change to more stable conformers, such as the latent form. We investigated conformational change in tengpin, an unusual prokaryotic serpin from the extremophile Thermoanaerobacter tengcongensis. In addition to the serpin domain, tengpin contains a functionally uncharacterized 56-amino-acid amino-terminal region. Deletion of this domain creates a variant--tengpinDelta51--which folds past the native state and readily adopts the latent conformation. Analysis of crystal structures together with mutagenesis studies show that the N terminus of tengpin protects a hydrophobic patch in the serpin domain and functions to trap tengpin in its native metastable state. A 13-amino-acid peptide derived from the N terminus is able to mimick the role of the N terminus in stabilizing the native state of tengpinDelta51. Therefore, the function of the N terminus in tengpin resembles protein cofactors that prevent mammalian serpins from spontaneously adopting the latent conformation.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17557112}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17557112 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17557112}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zhang, Q W.]] | | [[Category: Zhang, Q W.]] |
| [[Category: Serpin]] | | [[Category: Serpin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:57:39 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:35:47 2008'' |
