HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold

被引:54
作者
Callebaut, I
Gilgès, D
Vigon, I
Mornon, JP
机构
[1] Univ Paris 06, CNRS UMR 7590, LMCP, F-75252 Paris 05, France
[2] Univ Paris 07, CNRS UMR 7590, LMCP, F-75252 Paris, France
[3] Hop Henri Mondor, INSERM U474, F-94010 Creteil, France
关键词
adhesion; complement control protein; fibronectin type III; hyalin; hydrophobic cluster analysis; iterative database search; polycystic kidney disease;
D O I
10.1110/ps.9.7.1382
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Domains belonging to the immunoglobulin-like fold are responsible for a wide variety of molecular recognition processes. Here we describe a new family of domains, the HYR family, which is predicted to belong to this fold, and which appears to be involved in cellular adhesion. HYR domains were identified in several eukaryotic proteins, often associated with Complement Control Protein (CCP) modules or arranged in multiple copies. Our analysis provides a sequence and structural basis for understanding the role of these domains in interaction mechanisms and leads to further characterization of heretofore undescribed repeated domains with similar folds found in several bacterial proteins involved in enzymatic activities (some chitinases) or in cell surface adhesion (streptococcal C-alpha antigen).
引用
收藏
页码:1382 / 1390
页数:9
相关论文
共 39 条
[1]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[2]   Iterated profile searches with PSI-BLAST - a tool for discovery in protein databases [J].
Altschul, SF ;
Koonin, EV .
TRENDS IN BIOCHEMICAL SCIENCES, 1998, 23 (11) :444-447
[3]   SOLUTION STRUCTURE OF A PAIR OF COMPLEMENT MODULES BY NUCLEAR-MAGNETIC-RESONANCE [J].
BARLOW, PN ;
STEINKASSERER, A ;
NORMAN, DG ;
KIEFFER, B ;
WILES, AP ;
SIM, RB ;
CAMPBELL, ID .
JOURNAL OF MOLECULAR BIOLOGY, 1993, 232 (01) :268-284
[4]   H-1-NMR ASSIGNMENT AND SECONDARY STRUCTURE OF THE CELL-ADHESION TYPE-III MODULE OF FIBRONECTIN [J].
BARON, M ;
MAIN, AL ;
DRISCOLL, PC ;
MARDON, HJ ;
BOYD, J ;
CAMPBELL, ID .
BIOCHEMISTRY, 1992, 31 (07) :2068-2073
[5]   Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins [J].
Bateman, A ;
Birney, E ;
Durbin, R ;
Eddy, SR ;
Finn, RD ;
Sonnhammer, ELL .
NUCLEIC ACIDS RESEARCH, 1999, 27 (01) :260-262
[6]   CRYSTAL-STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL-ADHESION MOLECULE CD2 AT 2.5-ANGSTROM RESOLUTION [J].
BODIAN, DL ;
JONES, EY ;
HARLOS, K ;
STUART, DI ;
DAVIS, SJ .
STRUCTURE, 1994, 2 (08) :755-766
[7]   PROPOSED ACQUISITION OF AN ANIMAL PROTEIN DOMAIN BY BACTERIA [J].
BORK, P ;
DOOLITTLE, RF .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (19) :8990-8994
[8]  
BORK P, 1994, J MOL BIOL, V242, P309, DOI 10.1006/jmbi.1994.1582
[9]   Structure and distribution of modules in extracellular proteins [J].
Bork, P ;
Downing, AK ;
Kieffer, B ;
Campbell, ID .
QUARTERLY REVIEWS OF BIOPHYSICS, 1996, 29 (02) :119-167
[10]  
BORK P, 1995, TRENDS BIOCH SCI, V20