HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Patthy, L. Search for Related Content PubMed PubMed Citation Articles by Patthy, L. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 266, Issue 10, 6035-6037, 04, 1991

Homology of the precursor of pulmonary surfactant-associated protein SP- B with prosaposin and sulfated glycoprotein 1

L Patthy
Institute of Enzymology, Hungarian Academy of Sciences, Hungary.

The precursor of pulmonary surfactant-associated protein, SP-B, is composed of an NH2-terminal domain of 30 residues (a-type domain) and three tandem repeats of about 90 residues (b-type domain); biophysically active mature SP-B corresponds to the second b-type repeat. Consensus sequences constructed for the b-type repeats were used to search the data base for homologous sequences, and the search has revealed that prosaposin and sulfated glycoprotein 1 show a remarkable homology with these repeats. The domain organizations of the latter proteins, however, differ from that of SP-B precursor inasmuch as they contain four tandem copies of the b-type domain and a-type domains are present both in the NH2-terminal and COOH-terminal parts of the proteins. The implications of the homology of saposins and SP-B for their structure and function are discussed.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. A. Ryan, H. T. Akinbi, A. G. Serrano, J. Perez-Gil, H. Wu, F. X. McCormack, and T. E. Weaver Antimicrobial Activity of Native and Synthetic Surfactant Protein B Peptides J. Immunol., January 1, 2006; 176(1): 416 - 425. [Abstract] [Full Text] [PDF]

				C. R. Flach, P. Cai, D. Dieudonne, J. W. Brauner, K. M. W. Keough, J. Stewart, and R. Mendelsohn Location of Structural Transitions in an Isotopically Labeled Lung Surfactant SP-B Peptide by IRRAS Biophys. J., July 1, 2003; 85(1): 340 - 349. [Abstract] [Full Text] [PDF]

				S. M. Pietschmann and U. Pison cDNA cloning of ovine pulmonary SP-A, SP-B, and SP-C: isolation of two different sequences for SP-B Am J Physiol Lung Cell Mol Physiol, April 1, 2000; 278(4): L765 - L778. [Abstract] [Full Text] [PDF]

				A. M. Vaccaro, R. Salvioli, A. Barca, M. Tatti, F. Ciaffoni, B. Maras, R. Siciliano, F. Zappacosta, A. Amoresano, and P. Pucci Structural Analysis of Saposin C and B J. Biol. Chem., April 28, 1995; 270(17): 9953 - 9960. [Abstract] [Full Text] [PDF]