Domain motions in proteins

Abstract Although proteins require and possess well defined spatial structures, ever more cases are emerging where parts of proteins have moved relative to each other. These parts can be as small as single side chains or as large as domains of 50–150 residues. Analysis of these motions yields valuable data on the functions of the respective proteins.

[1]  R. Dixon,et al.  Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-A resolution. , 1991, The Journal of biological chemistry.

[2]  B. Matthews,et al.  A mutant T4 lysozyme displays five different crystal conformations , 1990, Nature.

[3]  Edward N. Baker,et al.  Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins , 1990, Nature.

[4]  G. Schulz,et al.  Induced-fit movements in adenylate kinases. , 1990, Faraday discussions.

[5]  T. Steitz,et al.  Glucose-induced conformational change in yeast hexokinase. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[6]  C. Thaller,et al.  The open/closed conformational equilibrium of aspartate aminotransferase. Studies in the crystalline state and with a fluorescent probe in solution. , 1991, European journal of biochemistry.

[7]  G. Schulz,et al.  The three‐dimensional structure of glutathione reductase from Escherichia coli at 3.0 Å resolution , 1991, Proteins.

[8]  I. Simon,et al.  The effect of iron binding on the conformation of transferrin. A small angle x-ray scattering study. , 1985, Biophysical journal.

[9]  L. Thim,et al.  A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex , 1991, Nature.

[10]  F. Quiocho,et al.  The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. , 1992 .

[11]  R. Stevens,et al.  Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution. , 1990, Biochemistry.

[12]  A Wlodawer,et al.  Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor. , 1991, Biochemistry.

[13]  R. Huber,et al.  The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution Implications for membrane binding and calcium channel activity , 1990, FEBS letters.

[14]  R. Huber,et al.  Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. , 1984, Journal of molecular biology.

[15]  N Go,et al.  Normal mode analysis of human lysozyme: Study of the relative motion of the two domains and characterization of the harmonic motion , 1991, Proteins.

[16]  H. Watson,et al.  A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement. , 1991, European journal of biochemistry.

[17]  J. Kuriyan,et al.  Convergent evolution of similar function in two structurally divergent enzymes , 1991, Nature.

[18]  W. Kabsch,et al.  Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607 , 1991, Nature.

[19]  H. Jhoti,et al.  High‐resolution X‐ray studies on rabbit serum transferrin: preliminary structure analysis of the N‐terminal half‐molecule at 2.3 Å resolution , 1990 .

[20]  K. Diederichs,et al.  The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 A resolution. , 1991, Journal of molecular biology.

[21]  F. Winkler,et al.  Structure of human pancreatic lipase , 1990, Nature.

[22]  E. Lattman,et al.  The mutation β99 Asp‐Tyr stabilizes Y—A new, composite quaternary state of human hemoglobin , 1991, Proteins.

[23]  F. Quiocho,et al.  Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. , 1989, Journal of molecular biology.

[24]  D. Blow,et al.  Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution. , 1991, Journal of molecular biology.

[25]  R. Huber,et al.  The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. , 1990, The EMBO journal.

[26]  M Karplus,et al.  Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. , 1990, Science.

[27]  W. Lipscomb,et al.  Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[28]  F. Quiocho,et al.  Structure of the L-leucine-binding protein refined at 2.4 A resolution and comparison with the Leu/Ile/Val-binding protein structure. , 1989, Journal of molecular biology.

[29]  L. Norskov,et al.  A serine protease triad forms the catalytic centre of a triacylglycerol lipase , 1990, Nature.

[30]  J. C. Martin,et al.  Domain communication in the dynamical structure of human immunodeficiency virus 1 protease. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[31]  G. Schulz,et al.  Structure of the complex of adenylate kinase from Escherichia coli with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate. , 1988, Journal of molecular biology.

[32]  R. Stevens,et al.  Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH. , 1990, Biochemistry.