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Anti-HIV and anti-tumor protein MAP30, a 30 kDa single-strand type-I RIP, shares similar secondary structure and β-sheet topology with the A chain of ricin, a type-II RIP

Published online by Cambridge University Press:  01 January 2000

YUN-XING WANG ,
JAISON JACOB ,
PAUL T. WINGFIELD ,
IRA PALMER ,
STEPHEN J. STAHL ,
JOSHUA D. KAUFMAN ,
PHILIP LIN HUANG ,
PAUL LEE HUANG ,
SYLVIA LEE-HUANG  and
DENNIS A. TORCHIA
YUN-XING WANG
Affiliation:
Molecular Structural Biology Core, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892
JAISON JACOB
Affiliation:
Molecular Structural Biology Core, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892
PAUL T. WINGFIELD
Affiliation:
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892
IRA PALMER
Affiliation:
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892
STEPHEN J. STAHL
Affiliation:
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892
JOSHUA D. KAUFMAN
Affiliation:
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892
PHILIP LIN HUANG
Affiliation:
Department of Biochemistry, School of Medicine, New York University, New York, New York 10016
PAUL LEE HUANG
Affiliation:
Department of Biochemistry, School of Medicine, New York University, New York, New York 10016
SYLVIA LEE-HUANG
Affiliation:
Department of Biochemistry, School of Medicine, New York University, New York, New York 10016
DENNIS A. TORCHIA
Affiliation:
Molecular Structural Biology Core, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892
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Abstract

MAP30 is a 30 kDa single-stranded, type-I ribosome inactivating protein (RIP) possessing anti-tumor and anti-HIV activities. It binds both ribosomal RNA and the HIV-1 long-terminal repeat DNA. To understand the structural basis for MAP30 activities, we undertook the study of MAP30 by solution NMR spectroscopy. We report nearly complete 1H, 13C, and 15N chemical shift assignments of its 263 amino acids. Based upon an analysis of secondary 13C chemical shifts, 3JHNHA coupling constants, hydrogen exchange data, and nuclear Overhauser effect patterns, we find that the secondary structure and β-sheet topology of MAP30 are very similar to those of the ricin A chain, a subunit of the well-known type-II RIP, even though two proteins display distinct activities. We therefore suggest that MAP30 and ricin A chain share a similar three-dimensional fold, and that the reported functional differences between two proteins arise primarily from differences in local three-dimensional structure and other structural properties such as surface electrostatic potentials.

Keywords

anti-canceranti-HIVNMRRIP proteinssecondary structure
Type
Research Article
Information
Protein Science , Volume 9 , Issue 1 , January 2000 , pp. 138 - 144
Copyright
© 2000 The Protein Society

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