Molecular recognition in the assembly of collagens: Terminal noncollagenous domains are key recognition modules in the formation of triple-helical protomers

doi:10.1074/jbc.R600025200

HOME

QUICK SEARCH:

	Author:		Keyword(s):
Year:		Vol:		Page:

A more recent version of this article appeared on December 15, 2006

This Article

	Full Text (Accepted Manuscript)
	All Versions of this Article: 281/50/38117 most recent R600025200v1
	Submit a Letter to Editor
	Alert me when this article is cited
	Alert me when eLetters are posted
	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
	Request Permissions

Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Khoshnoodi, J.
	Articles by Hudson, B. G.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Khoshnoodi, J.
	Articles by Hudson, B. G.

Social Bookmarking

	What's this?

Papers In Press, published online ahead of print November 2, 2006
J. Biol. Chem, 10.1074/jbc.R600025200
Submitted on August 22, 2006
Revised on October 31, 2006
Accepted on November 2, 2006

Molecular recognition in the assembly of collagens: Terminal noncollagenous domains are key recognition modules in the formation of triple-helical protomers

Jamshid Khoshnoodi, Jean-Philippe Cartailler, Keith Alvares, Arthur Veis, and Billy G. Hudson

Dept. of Medicine, Vanderbilt University School of Medicine, Nashville, TN 37232-2372

Corresponding Author: billy.hudson{at}vanderbilt.edu

The a-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen types, is trimerization that selects, binds and registers cognate a-chains for assembly of triple-helical protomers that subsequently oligomerize into specific suprastructures. In this article, we review recent findings on the mechanism of chain selection and infer that terminal noncollagenous domains function as recognition modules in trimerization, and are therefore key determinants of specificity in the assembly of suprastructures. This mechanism is also illustrated with computer-generated animations.

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:

G. W. Wong, S. A. Krawczyk, C. Kitidis-Mitrokostas, G. Ge, E. Spooner, C. Hug, R. Gimeno, and H. F. Lodish
Identification and characterization of CTRP9, a novel secreted glycoprotein, from adipose tissue that reduces serum glucose in mice and forms heterotrimers with adiponectin
FASEB J, January 1, 2009; 23(1): 241 - 258.
[Abstract] [Full Text] [PDF]

J. S. Kang, S. Colon, T. Hellmark, Y. Sado, B. G. Hudson, and D.-B. Borza
Identification of Noncollagenous Sites Encoding Specific Interactions and Quaternary Assembly of {alpha}3{alpha}4{alpha}5(IV) Collagen: IMPLICATIONS FOR ALPORT GENE THERAPY
J. Biol. Chem., December 12, 2008; 283(50): 35070 - 35077.
[Abstract] [Full Text] [PDF]

R. M. Vanacore, A.-J. L. Ham, J.-P. Cartailler, M. Sundaramoorthy, P. Todd, V. Pedchenko, Y. Sado, D.-B. Borza, and B. G. Hudson
A Role for Collagen IV Cross-links in Conferring Immune Privilege to the Goodpasture Autoantigen: STRUCTURAL BASIS FOR THE CRYPTICITY OF B CELL EPITOPES
J. Biol. Chem., August 15, 2008; 283(33): 22737 - 22748.
[Abstract] [Full Text] [PDF]

J. Fitzgerald, C. Rich, F. H. Zhou, and U. Hansen
Three Novel Collagen VI Chains, {alpha}4(VI), {alpha}5(VI), and {alpha}6(VI)
J. Biol. Chem., July 18, 2008; 283(29): 20170 - 20180.
[Abstract] [Full Text] [PDF]

M. A. Cejas, W. A. Kinney, C. Chen, J. G. Vinter, H. R. Almond Jr., K. M. Balss, C. A. Maryanoff, U. Schmidt, M. Breslav, A. Mahan, et al.
Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions
PNAS, June 24, 2008; 105(25): 8513 - 8518.
[Abstract] [Full Text] [PDF]