Motion in Serpins [serpin]

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Classification Known Domain Motion, Partial Refolding of Structure [D-f-2]

Structures
1OVA Conformation 2 [ PartsList ]
1OVA Intact Ovalbumin [ PartsList ]
1DVM Pai1 (active)
1DVN Pai1 (latent)
5API Cleaved alpha1-antitrypsin
5API Conformation 1

Description
Translation at a helix-sheet interface results in the transformation of the tertiary structure by insertion of strand into sheet.
serpin existed for which both the cleaved and uncleaved structures were solved. Rather, uncleaved ovalbumin solved, but ovalbumin doesn't undergo transformation, and cleaved but not uncleaved alpha1-antitrypsin solved. Ovalbumin and alpha-1-antitrypsin 30% identity in aa sequence; Chotia says adequate to compare structures. Both serpins consist of two fragments. In cleaved alpha1-antirypsin, fragment 2 has moved 3.9 A and 6 degrees away from fragment 1 as compared with their positions in uncleaved ovalbumin, classifying motion as known shear mechanism. By 1994, several additional cleaved serpins (including plasminogen activator inhibitor-1, q.v.) and one additional uncleaved serpins had been solved (Wei et al.)

Particular values describing motion
Creation Date = 19970822
Modification Date = 19971212
Experimental Methods = x (Traditional x-ray)

References
P Stein and C Chothia (1991). Serpin Tertiary Structure Transformation. J. Mol. Biol. 221: 615-621. [Medline info for 94157914]
A Wei, H Rubin, B S Cooperman, and D W Christianson (1994). Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Struct. Biol. 1: 251-258. [Medline info for 94157914]
R J Fletterick and M E McGrath (1994). Deconvolution serpins. Struct. Biol. 1: 201-203. [Medline info for 94157914]
J Mottonen, A Strand, J Symersky, R M Sweet, D E Danley, K F Geoghegan, R D Gerard, E J Goldsmith (1992). Structural basis of latency in plasminogen activator inhibitor-1. Nature. 355:270-273. [Medline info for 94157914]
P Stein and C Chothia (1991). Serpin tertiary structure transformation. J. Mol. Biol. 221: 615-621. [Medline info for 94157914]
R A Engh, H T Wright and R Huber (1990). Modeling the intact form of the a1-proteinase inhibitor. Prot. Eng. 3: 469-477. [Medline info for 94157914]
H Loebermann, R Tokuoka, J Deisenhofer and R Huber (1984). Human a1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177: 531-556. [Medline info for 94157914]
J Mottonen, A Strand, J Symersky, R M Sweet, D E Danley, K F Goeghegan, R D Gerard and E J Goldsmith (1992). Structural basis of latency in plasminogen activator inhibitor-1. Nature. 355: 270-273. [Medline info for 94157914]

GO terms associated with structures
Molecular functionserine-type endopeptidase inhibitor activity

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Serpins 7api [ A ] 1psi [ A ] 372

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
33101-11910 alpha-1-antitrypsin 1psi [ A ] 1ezx [ A ] 335
830171-19785 PAI-1 (latency rxn) upload [ A ] upload [ A ] 402
828994-18394 PAI-1-latent upload [ A ] upload [ A ] 379
829046-18425 PAI-1-latent upload [ A ] upload [ A ] 379
672012-14342 Serine Proteinase In upload [ A ] upload [ A ] 373
906079-22266 Serpin (PAI-1) upload [ A ] upload [ A ] 373
46403-19382 serpin alpha-1 anti- upload [ B ] 1ezx [ A ] 335
557264-17894 Serpins 7api [ A ] 1psi [ A ] 372
65330-10757 testing 1dvn [ A ] 1dvm [ A ] 379


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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu