2aeb: Difference between revisions

Revision as of 03:27, 29 July 2008

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File:2aeb.png

Template:STRUCTURE 2aeb

Crystal structure of human arginase I at 1.29 A resolution and exploration of inhibition in immune response.Crystal structure of human arginase I at 1.29 A resolution and exploration of inhibition in immune response.

Template:ABSTRACT PUBMED 16141327

About this StructureAbout this Structure

2AEB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response., Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13058-63. Epub 2005 Sep 2. PMID:16141327

Human arginase II: crystal structure and physiological role in male and female sexual arousal., Cama E, Colleluori DM, Emig FA, Shin H, Kim SW, Kim NN, Traish AM, Ash DE, Christianson DW, Biochemistry. 2003 Jul 22;42(28):8445-51. PMID:12859189

Genetic knowledge client perspectives, and genetic counseling., Griffin ML, Kavanagh CM, Sorenson JR, Soc Work Health Care. 1976-1977 Winter;2(2):171-80. PMID:1052097

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of human arginase I at 1.29 A resolution and exploration of inhibition in immune response.'''
+===Crystal structure of human arginase I at 1.29 A resolution and exploration of inhibition in immune response.===
-==Overview==
+<!--
-Human arginase I is a potential target for therapeutic intervention in diseases linked to compromised l-arginine homeostasis. Here, we report high-affinity binding of the reaction coordinate analogue inhibitors 2(S)-amino-6-boronohexanoic acid (ABH, Kd = 5 nM) and S-(2-boronoethyl)-l-cysteine (BEC, Kd = 270 nM) to human arginase I, and we report x-ray crystal structures of the respective enzyme-inhibitor complexes at 1.29- and 1.94-A resolution determined from crystals twinned by hemihedry. The ultrahigh-resolution structure of the human arginase I-ABH complex yields an unprecedented view of the binuclear manganese cluster and illuminates the structural basis for nanomolar affinity: bidentate inner-sphere boronate-manganese coordination interactions and fully saturated hydrogen bond networks with inhibitor alpha-amino and alpha-carboxylate groups. These interactions are therefore implicated in the stabilization of the transition state for l-arginine hydrolysis. Electron density maps also reveal that active-site residue H141 is protonated as the imidazolium cation. The location of H141 is such that it could function as a general acid to protonate the leaving amino group of l-ornithine during catalysis, and this is a revised mechanistic proposal for arginase. This work serves as a foundation for studying the structural and chemical biology of arginase I in the immune response, and we demonstrate the inhibition of arginase activity by ABH in human and murine myeloid cells.
+The line below this paragraph, {{ABSTRACT_PUBMED_16141327}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16141327 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16141327}}
 ==About this Structure==
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 ==Reference==
 Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response., Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13058-63. Epub 2005 Sep 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16141327 16141327]
+Human arginase II: crystal structure and physiological role in male and female sexual arousal., Cama E, Colleluori DM, Emig FA, Shin H, Kim SW, Kim NN, Traish AM, Ash DE, Christianson DW, Biochemistry. 2003 Jul 22;42(28):8445-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12859189 12859189]
+Genetic knowledge client perspectives, and genetic counseling., Griffin ML, Kavanagh CM, Sorenson JR, Soc Work Health Care. 1976-1977 Winter;2(2):171-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1052097 1052097]
 [[Category: Arginase]]
 [[Category: Homo sapiens]]
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 [[Category: Hydrolase]]
 [[Category: Perfectly twinned crystal]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:56:19 2008''
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