Crystal structure of the MrkD1Preceptor binding domain ofKlebsiella pneumoniaeand identification of the human collagen V binding interface-Reference-Cited by-同舟云学术

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Crystal structure of the MrkD1Preceptor binding domain ofKlebsiella pneumoniaeand identification of the human collagen V binding interface

Published:2012-09-18 Issue:4 Volume:86 Page:882-893
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Molecular Microbiology

Author:

Rêgo Ana Toste¹,Johnson Jeremiah G.²,Geibel Sebastian¹,Enguita Francisco J.³,Clegg Steven²,Waksman Gabriel

Affiliation:

1. Institute of Structural and Molecular Biology; University College London and Birkbeck College; Malet Street; London; WC1E 7HX; UK

2. Department of Microbiology; College of Medicine; University of Iowa; Iowa City; Iowa; 52242; USA

3. Instituto de Medicina Molecular; Faculdade de Medicina; Universidade de Lisboa; Lisboa; Portugal

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Reference38 articles.

1. PHENIX: building new software for automated crystallographic structure determination;Adams;Acta Crystallogr D Biol Crystallogr,2002

2. Nucleotide sequence and functions of mrk determinants necessary for expression of type 3 fimbriae in Klebsiella pneumoniae;Allen;J Bacteriol,1991

3. Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin;Bouckaert;Mol Microbiol,2005

4. The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine;Buts;Mol Microbiol,2003

5. The CCP4 suite: programs for protein crystallography;CCP4;Acta Crystallogr D Biol Crystallogr,1994

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