Judy Luke

Author's posts

The role of protein dynamics in increasing binding affinity for an engineered protein-protein interaction established by H/D exchange mass spectrometry

Horn JR, Kraybill B, Petro EJ, Coales SJ, Morrow JA, Hamuro Y, Kossiakoff AA

Biochemistry 2006 Jul;45(28):8488-98

PMID: 16834322


It is generally accepted that protein and solvation dynamics play fundamental roles in the mechanisms of protein-protein binding; however, assessing their contribution meaningfully has not been straightforward. Here, hydrogen/deuterium exchange mass spectrometry (H/D-Ex) was employed …

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Crystal structure and site 1 binding energetics of human placental lactogen

Walsh ST, Kossiakoff AA

J. Mol. Biol. 2006 May;358(3):773-84

PMID: 16546209


In primates, placental lactogen (PL) is a pituitary hormone with fundamental roles during pregnancy involving fetal growth, metabolism, and stimulating lactation in the mother. Human placental lactogen (hPL) is highly conserved with human growth hormone (hGH) and both hormones bind to the hPRLR …

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Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis

Bang D, Gribenko AV, Tereshko V, Kossiakoff AA, Kent SB, Makhatadze GI

Nat. Chem. Biol. 2006 Mar;2(3):139-43

PMID: 16446709


The alpha-helix is a fundamental protein structural motif and is frequently terminated by a glycine residue. Explanations for the predominance of glycine at the C-cap terminal portions of alpha-helices have invoked uniquely favorable energetics of …

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Structure of bistramide A-actin complex at a 1.35 angstroms resolution

Rizvi SA, Tereshko V, Kossiakoff AA, Kozmin SA

J. Am. Chem. Soc. 2006 Mar;128(12):3882-3

PMID: 16551075


Bistramide A is a highly potent antiproliferative marine natural product from Lissoclinum bistratum. We have previously established actin as the primary cellular receptor of bistramide A. We report herein the X-ray structure of bistramide A bound to monomeric …

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The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold

Qiu Y, Tereshko V, Kim Y, Zhang R, Collart F, Yousef M, Kossiakoff A, Joachimiak A

Proteins 2006 Jan;62(1):8-16

PMID: 16287087


The structure of Aq_328, an uncharacterized protein from hyperthermophilic bacteria Aquifex aeolicus, has been determined to 1.9 A by using multi-wavelength anomalous diffraction (MAD) phasing. Although the amino acid sequence analysis shows that …

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Alternative views of functional protein binding epitopes obtained by combinatorial shotgun scanning mutagenesis

Pál G, Fong SY, Kossiakoff AA, Sidhu SS

Protein Sci. 2005 Sep;14(9):2405-13

PMID: 16131663


Combinatorial shotgun scanning mutagenesis was used to analyze two large, related protein binding sites to assess the specificity and importance of individual side chain contributions to binding affinity. The strategy allowed for cost-effective generation of a plethora of functional data. …

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Shotgun alanine scanning shows that growth hormone can bind productively to its receptor through a drastically minimized interface

Kouadio JL, Horn JR, Pal G, Kossiakoff AA

J. Biol. Chem. 2005 Jul;280(27):25524-32

PMID: 15857837


The high affinity binding site (Site1) of the human growth hormone (hGH) binds to its cognate receptor (hGHR) via a concave surface patch containing about 35 residues. Using 167 sequences from a shotgun alanine scanning analysis of Site1, we …

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Total chemical synthesis and X-ray crystal structure of a protein diastereomer: [D-Gln 35]ubiquitin

Bang D, Makhatadze GI, Tereshko V, Kossiakoff AA, Kent SB

Angew. Chem. Int. Ed. Engl. 2005 Jun;44(25):3852-6

PMID: 15834850


Intramolecular cooperativity in a protein binding site assessed by combinatorial shotgun scanning mutagenesis

Pál G, Ultsch MH, Clark KP, Currell B, Kossiakoff AA, Sidhu SS

J. Mol. Biol. 2005 Apr;347(3):489-94

PMID: 15755445


Combinatorial shotgun alanine-scanning was used to assess intramolecular cooperativity in the high affinity site (site 1) of human growth hormone (hGH) for binding to its receptor. A total of 19 side-chains were analyzed and statistically …

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The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s)

Gopal B, Madan LL, Betz SF, Kossiakoff AA

Biochemistry 2005 Jan;44(1):193-201

PMID: 15628860


Common structural motifs, such as the cupin domains, are found in enzymes performing different biochemical functions while retaining a similar active site configuration and structural scaffold. The soil bacterium Bacillus subtilis has 20 cupin genes (0.5% of the total genome) with …

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