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
[21]   The PROSITE database, its status in 1999 [J].
Hofmann, K ;
Bucher, P ;
Falquet, L ;
Bairoch, A .
NUCLEIC ACIDS RESEARCH, 1999, 27 (01) :215-219
[22]   CRYSTAL-STRUCTURE OF TANDEM TYPE-III FIBRONECTIN DOMAINS FROM DROSOPHILA NEUROGLIAN AT 2.0 ANGSTROM [J].
HUBER, AH ;
WANG, YME ;
BIEBER, AJ ;
BJORKMAN, PJ .
NEURON, 1994, 12 (04) :717-731
[23]   Three-dimensional structure of cell adhesion molecules [J].
Jones, EY .
CURRENT OPINION IN CELL BIOLOGY, 1996, 8 (05) :602-608
[24]  
JONES JP, 1995, J MARK COMMUN, V1, P1
[25]  
KRAULIS PJ, 1991, J APPL CRYSTALLOGR, V12, P283
[26]   STRUCTURE OF A FIBRONECTIN TYPE-III DOMAIN FROM TENASCIN PHASED BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN [J].
LEAHY, DJ ;
HENDRICKSON, WA ;
AUKHIL, I ;
ERICKSON, HP .
SCIENCE, 1992, 258 (5084) :987-991
[27]   TRACING THE SPREAD OF FIBRONECTIN TYPE-III DOMAINS IN BACTERIAL GLYCOHYDROLASES [J].
LITTLE, E ;
BORK, P ;
DOOLITTLE, RF .
JOURNAL OF MOLECULAR EVOLUTION, 1994, 39 (06) :631-643
[28]   A GENE (SRPX) ENCODING A SUSHI-REPEAT-CONTAINING PROTEIN IS DELETED IN PATIENTS WITH X-LINKED RETINITIS-PIGMENTOSA [J].
MEINDL, A ;
CARVALHO, MRS ;
HERRMANN, K ;
LORENZ, B ;
ACHATZ, H ;
LORENZ, B ;
APFELSTEDTSYLLA, E ;
WITTWER, B ;
ROSS, M ;
MEITINGER, T .
HUMAN MOLECULAR GENETICS, 1995, 4 (12) :2339-2346
[29]   SOLUTION STRUCTURE OF THE EPITHELIAL CADHERIN DOMAIN RESPONSIBLE FOR SELECTIVE CELL-ADHESION [J].
OVERDUIN, M ;
HARVEY, TS ;
BAGBY, S ;
TONG, KI ;
YAU, P ;
TAKEICHI, M ;
IKURA, M .
SCIENCE, 1995, 267 (5196) :386-389
[30]   SMART: identification and annotation of domains from signalling and extracellular protein sequences [J].
Ponting, CP ;
Schultz, J ;
Milpetz, F ;
Bork, P .
NUCLEIC ACIDS RESEARCH, 1999, 27 (01) :229-232