PMID- 10543983
OWN - NLM
STAT- MEDLINE
DCOM- 19991222
LR  - 20061115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 264
IP  - 3
DP  - 1999 Nov 2
TI  - Characteristics of fibrinogen binding to the domain of CD11c, an alpha subunit of
      p150,95.
PG  - 630-4
AB  - beta2 integrins on leukocytes play important roles on cell-cell or cell-matrix
      adhesion through their ability to bind multiple ligands. The alpha subunits of
      leukocyte CD11/CD18 integrins contain an approximately 200-amino-acid inserted
      domain (I-domain) which is implicated in ligand binding function. To understand
      the characteristics of ligand binding to the alpha subunit of beta2 integrin
      p150,95 (CD11c/CD18), a recombinant form of the I-domain of CD11c was generated
      and analyzed for the interaction with fibrinogen, one of the ligands of p150,95. 
      It was found that the CD11c I-domain bound fibrinogen specifically. Fibrinogen
      binding to the CD11c I-domain was inhibited by a molar excess of fragment E, a
      central domain of fibrinogen, and not by that of fragment D, a distal domain of
      fibrinogen, suggesting that CD11c/CD18 recognizes a central domain of fibrinogen.
      Divalent cations such as Mg(2+) and Mn(2+) were required for fibrinogen binding
      to the CD11c I-domain. Also alanine substitutions on the putative metal binding
      sites of the CD11c I-domain such as Asp(242) and Tyr(209) reduced its ability to 
      bind fibrinogen. These data reinforce the fact that the divalent cation is a
      prerequisite for ligand binding of the CD11c I-domain.
CI  - Copyright 1999 Academic Press.
FAU - Nham, S U
AU  - Nham SU
AD  - Biology Group, Division of Science Education, Kangwon National University,
      Choonchun, Kangwon, 200-701, Korea. sunham@cc.kangwon.ac.kr
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Integrin alphaXbeta2)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 9001-32-5 (Fibrinogen)
SB  - IM
MH  - Amino Acid Substitution
MH  - Binding Sites/genetics
MH  - Fibrinogen/*chemistry/metabolism
MH  - Humans
MH  - Integrin alphaXbeta2/*chemistry/metabolism
MH  - Protein Binding
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Structure-Activity Relationship
EDAT- 1999/11/02 00:00
MHDA- 1999/11/02 00:01
CRDT- 1999/11/02 00:00
PHST- 1999/11/02 00:00 [pubmed]
PHST- 1999/11/02 00:01 [medline]
PHST- 1999/11/02 00:00 [entrez]
AID - 10.1006/bbrc.1999.1564 [doi]
AID - S0006-291X(99)91564-4 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Nov 2;264(3):630-4. doi: 10.1006/bbrc.1999.1564.