JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Resnick, D.
Right arrow Articles by Krieger, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Resnick, D.
Right arrow Articles by Krieger, M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 271, Number 43, Issue of October 25, 1996 pp. 26924-26930
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Structures of Class A Macrophage Scavenger Receptors
ELECTRON MICROSCOPIC STUDY OF FLEXIBLE, MULTIDOMAIN, FIBROUS PROTEINS AND DETERMINATION OF THE DISULFIDE BOND PATTERN OF THE SCAVENGER RECEPTOR CYSTEINE-RICH DOMAIN

(Received for publication, April 2, 1996, and in revised form, June 14, 1996)

David Resnick Dagger , Jon E. Chatterton Dagger , Karen Schwartz , Henry Slayter '' and Monty Krieger Dagger

From the Dagger  Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139,  Arris Pharmaceutical Corporation, South San Francisco, California 94080, and the '' Dana-Farber Cancer Institute, Boston, Massachusetts 02115

Structures of secreted forms of the human type I and II class A macrophage scavenger receptors were studied using biochemical and biophysical methods. Proteolytic analysis was used to determine the intramolecular disulfide bonds in the type I-specific scavenger receptor cysteine-rich (SRCR) domain: Cys2-Cys7, Cys3-Cys8, and Cys5-Cys6. This pattern is likely to be shared by the highly homologous domains in the many other members of the SRCR domain superfamily. Electron microscopy using rotary shadowing and negative staining showed that the type I and II receptors are extended molecules whose contour lengths are ~440 Å. They comprised two adjacent fibrous segments, an alpha -helical coiled-coil (~230 Å, including a contribution from the N-terminal spacer domain) and a collagenous triple helix (~210 Å). The type I molecules also contained a C-terminal globular structure (~58 × 76 Å) composed of three SRCR domains. The fibrous domains were joined by an extremely flexible hinge. The angle between these domains varied from 0 to 180° and depended on the conditions of sample preparation. Unexpectedly, at physiologic pH, the prevalent angle seen using rotary shadowing was 0°, resulting in a structure that is significantly more compact than previously suggested. The apparent juxtaposition of the fibrous domains at neutral pH provides a framework for future structure-function studies of these unusual multiligand receptors.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Y. Chen, M. Sankala, J. R. M. Ojala, Y. Sun, A. Tuuttila, D. E. Isenman, K. Tryggvason, and T. Pikkarainen
A Phage Display Screen and Binding Studies with Acetylated Low Density Lipoprotein Provide Evidence for the Importance of the Scavenger Receptor Cysteine-rich (SRCR) Domain in the Ligand-binding Function of MARCO
J. Biol. Chem., May 5, 2006; 281(18): 12767 - 12775.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
J. H. Brown
Breaking symmetry in protein dimers: designs and functions.
Protein Sci., January 1, 2006; 15(1): 1 - 13.
[Abstract] [Full Text] [PDF]

Home page
 J. Leukoc. Biol.Home page
B. B. Gowen, T. K. Borg, A. Ghaffar, and E. P. Mayer
The collagenous domain of class A scavenger receptors is involved in macrophage adhesion to collagens
J. Leukoc. Biol., April 1, 2001; 69(4): 575 - 582.
[Abstract] [Full Text]

Home page
 J. Lipid Res.Home page
A. Daugherty, S. C. Whitman, A. E. Block, and D. L. Rateri
Polymorphism of class A scavenger receptors in C57BL/6 mice
J. Lipid Res., October 1, 2000; 41(10): 1568 - 1577.
[Abstract] [Full Text]

Home page
 Infect. Immun.Home page
L. Peiser, P. J. Gough, T. Kodama, and S. Gordon
Macrophage Class A Scavenger Receptor-Mediated Phagocytosis of Escherichia coli: Role of Cell Heterogeneity, Microbial Strain, and Culture Conditions In Vitro
Infect. Immun., April 1, 2000; 68(4): 1953 - 1963.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
J. Takito, L. Yan, J. Ma, C. Hikita, S. Vijayakumar, D. Warburton, and Q. Al-Awqati
Hensin, the polarity reversal protein, is encoded by DMBT1, a gene frequently deleted in malignant gliomas
Am J Physiol Renal Physiol, August 1, 1999; 277(2): F277 - F289.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Hikita, J. Takito, S. Vijayakumar, and Q. Al-Awqati
Only Multimeric Hensin Located in the Extracellular Matrix Can Induce Apical Endocytosis and Reverse the Polarity of Intercalated Cells
J. Biol. Chem., June 18, 1999; 274(25): 17671 - 17676.
[Abstract] [Full Text] [PDF]

Home page
 J. Pharmacol. Exp. Ther.Home page
P. G. Lysko, J. Weinstock, C. L. Webb, M. E. Brawner, and N. A. Elshourbagy
Identification of a Small-Molecule, Nonpeptide Macrophage Scavenger Receptor Antagonist
J. Pharmacol. Exp. Ther., June 1, 1999; 289(3): 1277 - 1285.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
J. Belkner, H. Stender, and H. Kuhn
The Rabbit 15-Lipoxygenase Preferentially Oxygenates LDL Cholesterol Esters, and This Reaction Does Not Require Vitamin E
J. Biol. Chem., September 4, 1998; 273(36): 23225 - 23232.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Andersson and M. W. Freeman
Functional Changes in Scavenger Receptor Binding Conformation Are Induced by Charge Mutants Spanning the Entire Collagen Domain
J. Biol. Chem., July 31, 1998; 273(31): 19592 - 19601.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
P. J. Gough, D. R. Greaves, and S. Gordon
A naturally occurring isoform of the human macrophage scavenger receptor (SR-A) gene generated by alternative splicing blocks modified LDL uptake
J. Lipid Res., March 1, 1998; 39(3): 531 - 543.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
O. Elomaa, M. Sankala, T. Pikkarainen, U. Bergmann, A. Tuuttila, A. Raatikainen-Ahokas, H. Sariola, and K. Tryggvason
Structure of the Human Macrophage MARCO Receptor and Characterization of Its Bacteria-binding Region
J. Biol. Chem., February 20, 1998; 273(8): 4530 - 4538.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Hu, O. Hauache, and A. M. Spiegel
Human Ca2+ Receptor Cysteine-rich Domain. ANALYSIS OF FUNCTION OF MUTANT AND CHIMERIC RECEPTORS
J. Biol. Chem., May 19, 2000; 275(21): 16382 - 16389.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. D. Hooper, J. A. Clements, J. P. Quigley, and T. M. Antalis
Type II Transmembrane Serine Proteases. INSIGHTS INTO AN EMERGING CLASS OF CELL SURFACE PROTEOLYTIC ENZYMES*
J. Biol. Chem., January 5, 2001; 276(2): 857 - 860.
[Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.