Výsledky vyhledávání

Deciphering the Hidden Informational Content of Protein Sequences

Autor: Michael A. Weiss, Yanwu Yang, Sunil Evan Saith, Wenhua Jia, Qing Xin Hua, Ming Liu, Shi Quan Hu, Peter Arvan, Jonathan Whittaker

Publikováno v: Journal of Biological Chemistry. 285:30989-31001

Protein sequences encode both structure and foldability. Whereas the interrelationship of sequence and structure has been extensively investigated, the origins of folding efficiency are enigmatic. We demonstrate that the folding of proinsulin require

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d11b6127be1cb3b629cabd00c9914a75
https://doi.org/10.1074/jbc.m110.152645

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Supramolecular Protein Engineering

Autor: Nelson B. Phillips, Michael A. Weiss, Qing Xin Hua, Faramarz Ismail-Beigi, Jonathan Whittaker, Zhu Li Wan, Kun Huang, Linda Whittaker, Shi Quan Hu

Publikováno v: Journal of Biological Chemistry. 285:11755-11759

Bottom-up control of supramolecular protein assembly can provide a therapeutic nanobiotechnology. We demonstrate that the pharmacological properties of insulin can be enhanced by design of “zinc staples” between hexamers. Paired (i, i+4) His subs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::373891fc4c438315c2152ddf7916df51
https://doi.org/10.1074/jbc.c110.105825

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An Achilles' Heel in an Amyloidogenic Protein and Its Repair

Autor: Robert Tycko, Yanwu Yang, Michael A. Weiss, Faramarz Ismail-Beigi, Panayotis G. Katsoyannis, Aneta T. Petkova, Bin Xu, Robert B. Mackin, Nelson B. Phillips, Jonathan Whittaker, Ying-Chi Chu, Qing-xin Hua, Kun Huang, Shi-Quan Hu, I-Ju Ye

Publikováno v: Journal of Biological Chemistry. 285:10806-10821

Insulin fibrillation provides a model for a broad class of amyloidogenic diseases. Conformational distortion of the native monomer leads to aggregation-coupled misfolding. Whereas β-cells are protected from proteotoxicity by hexamer assembly, fibril

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c95faf22a5d3c763db5a752b6d197100
https://doi.org/10.1074/jbc.m109.067850

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Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists

Autor: Geoffrey K.-W. Kong, John G. Menting, Satoe Nakagawa, Brian J. Smith, Michael C. Lawrence, Colin W. Ward, Panayotis G. Katsoyannis, Jonathan Whittaker, Shu Jin Chan, Shi Quan Hu, Kun Huang, Michael A. Weiss, Donald F. Steiner

Publikováno v: Proceedings of the National Academy of Sciences. 107:6771-6776

The C-terminal segment of the human insulin receptor α-chain (designated αCT) is critical to insulin binding as has been previously demonstrated by alanine scanning mutagenesis and photo-cross-linking. To date no information regarding the structure

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62c549ebd194b88fc56e7a04afa7b739
https://doi.org/10.1073/pnas.1001813107

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Contribution of Residue B5 to the Folding and Function of Insulin and IGF-I

Autor: Michael A. Weiss, Ming Liu, Linda Whittaker, Charles T. Roberts, Peter Arvan, Aubree A. Ng, Nelson B. Phillips, Stephen B. H. Kent, Youhei Sohma, Jonathan Whittaker, Qing Xin Hua, Shi Quan Hu

Publikováno v: Journal of Biological Chemistry. 285:5040-5055

Proinsulin exhibits a single structure, whereas insulin-like growth factors refold as two disulfide isomers in equilibrium. Native insulin-related growth factor (IGF)-I has canonical cystines (A6—A11, A7–B7, and A20—B19) maintained by IGF-bindi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b87f4a0507e50f0cdbfcc400440f1bca
https://doi.org/10.1074/jbc.m109.062992

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Enhancing the Activity of a Protein by Stereospecific Unfolding

Autor: Panayotis G. Katsoyannis, Shuhua Wang, Michael A. Weiss, Satoe Nakagawa, Wenhua Jia, Qing Xin Hua, Shi Quan Hu, Jonathan Whittaker, Bin Xu, Kun Huang

Publikováno v: Journal of Biological Chemistry. 284:14586-14596

A central tenet of molecular biology holds that the function of a protein is mediated by its structure. An inactive ground-state conformation may nonetheless be enjoined by the interplay of competing biological constraints. A model is provided by ins

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f98944a8be78e0dd0b1340f023708c36
https://doi.org/10.1074/jbc.m900085200

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Decoding the Cryptic Active Conformation of a Protein by Synthetic Photoscanning

Autor: Jonathan Whittaker, Run Ying Wang, Shuhua Wang, Satoe Nakagawa, Michael A. Weiss, Shi Quan Hu, Ying Chi Chu, Bin Xu, Panayotis G. Katsoyannis, Kun Huang

Publikováno v: Journal of Biological Chemistry. 284:14597-14608

Proteins evolve in a fitness landscape encompassing a complex network of biological constraints. Because of the interrelation of folding, function, and regulation, the ground-state structure of a protein may be inactive. A model is provided by insuli

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e022a9be140773ea447ba2c2f1a9e877
https://doi.org/10.1074/jbc.m900087200

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The Structure of a Mutant Insulin Uncouples Receptor Binding from Protein Allostery

Autor: Kun Huang, Jonathan Whittaker, Zhu Li Wan, Shi Quan Hu, Michael A. Weiss

Publikováno v: Journal of Biological Chemistry. 283:21198-21210

The zinc insulin hexamer undergoes allosteric reorganization among three conformational states, designated T(6), T(3)R(3)(f), and R(6). Although the free monomer in solution (the active species) resembles the classical T-state, an R-like conformation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::598d61526850eadd11801c1fcdaed8fd
https://doi.org/10.1074/jbc.m800235200

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Toward the Active Conformation of Insulin

Autor: Michael A. Weiss, Shuhua Wang, Satoe Nakagawa, Qing Xin Hua, Wenhua Jia, Shi Quan Hu

Publikováno v: Journal of Biological Chemistry. 281:24900-24909

How insulin binds to the insulin receptor has long been a subject of speculation. Although the structure of the free hormone has been extensively characterized, a variety of evidence suggests that a conformational change occurs upon receptor binding.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3750cfaef93ebd9faea10318c2369ef0
https://doi.org/10.1074/jbc.m602691200

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Chiral Mutagenesis of Insulin

Autor: Michael A. Weiss, Shi Quan Hu, Panayotis G. Katsoyannis, Satoe H. Nakagawa, Qing Xin Hua, Wenhua Jia, Shuhua Wang

Publikováno v: Journal of Biological Chemistry. 281:22386-22396

Insulin contains a β-turn (residues B20-B23) interposed between two receptor-binding elements, the central α-helix of the B chain (B9-B19) and its C-terminal β-strand (B24-B28). The turn contains conserved glycines at B20 and B23. Although insulin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e82d47ad8bb66c899adcf22013ab09f8
https://doi.org/10.1074/jbc.m603547200

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