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Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
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Tegoni M, Ramoni R, Bignetti E, Spinelli S, Cambillau C. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nat Struct Biol. 3:1996;863-867.
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(1996)
Nat Struct Biol
, vol.3
, pp. 863-867
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Tegoni, M.1
Ramoni, R.2
Bignetti, E.3
Spinelli, S.4
Cambillau, C.5
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52
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0029858390
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The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition
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Bianchet MA, Bains G, Pelosi P, Pevsner J, Snyder SH, Monaco HL, Amzel LM. The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition. Nat Struct Biol. 3:1996;934-939.
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(1996)
Nat Struct Biol
, vol.3
, pp. 934-939
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Bianchet, M.A.1
Bains, G.2
Pelosi, P.3
Pevsner, J.4
Snyder, S.H.5
Monaco, H.L.6
Amzel, L.M.7
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53
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0029092779
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One-step evolution of a dimer from a monomeric protein
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This paper presents the structure of a mutant of monomeric staphylococcal nuclease and describes how the deletion of a six amino acid surface loop transforms a monomer into a very stable dimer. The deletion prevents the C-terminal helix from folding back onto the same monomer such that it extends away from it, ready to associate with the other monomer in the dimer. of special interest
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Green SM, Gittis AG, Meeker AK, Lattman EE. One-step evolution of a dimer from a monomeric protein. Nat Struct Biol. 2:1995;746-751 This paper presents the structure of a mutant of monomeric staphylococcal nuclease and describes how the deletion of a six amino acid surface loop transforms a monomer into a very stable dimer. The deletion prevents the C-terminal helix from folding back onto the same monomer such that it extends away from it, ready to associate with the other monomer in the dimer. of special interest.
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(1995)
Nat Struct Biol
, vol.2
, pp. 746-751
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Green, S.M.1
Gittis, A.G.2
Meeker, A.K.3
Lattman, E.E.4
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54
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0029911754
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Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites
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This paper describes a dramatic movement of one of three domains in pyruvate phosphate dikinase; the phosphoinositide domain swivels between two states in order to bring a phosphor group from the active site of the nucleotide-binding domain to that of the PEP/pyruvate-binding domain. The phosphate group is moved over a distance of 45 Å involving a domain swivel motion of about 100° around a single residue. of outstanding interest
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Herzberg O, Chen CCH, Kapadia G, McGuire M, Carrol LJ, Noh SJ, Dunaway-Mariano D. Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites. Proc Natl Acad Sci USA. 93:1996;2652-2657 This paper describes a dramatic movement of one of three domains in pyruvate phosphate dikinase; the phosphoinositide domain swivels between two states in order to bring a phosphor group from the active site of the nucleotide-binding domain to that of the PEP/pyruvate-binding domain. The phosphate group is moved over a distance of 45 Å involving a domain swivel motion of about 100° around a single residue. of outstanding interest.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 2652-2657
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Herzberg, O.1
Chen, C.C.H.2
Kapadia, G.3
McGuire, M.4
Carrol, L.J.5
Noh, S.J.6
Dunaway-Mariano, D.7
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55
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0028360742
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Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer
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Wang J, Smerdon SJ, Jäger J, Kohlstaedt LA, Rice PA, Frieman JM, Steitz TA. Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer. Proc Natl Acad Sci USA. 91:1994;7242-7246.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 7242-7246
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Wang, J.1
Smerdon, S.J.2
Jäger, J.3
Kohlstaedt, L.A.4
Rice, P.A.5
Frieman, J.M.6
Steitz, T.A.7
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