PMID- 10380930
OWN - NLM
STAT- MEDLINE
DCOM- 19990722
LR  - 20220318
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 97
IP  - 6
DP  - 1999 Jun 11
TI  - Structure of a heterophilic adhesion complex between the human CD2 and CD58
      (LFA-3) counterreceptors.
PG  - 791-803
AB  - Interaction between CD2 and its counterreceptor, CD58 (LFA-3), on opposing cells 
      optimizes immune recognition, facilitating contacts between helper T lymphocytes 
      and antigen-presenting cells as well as between cytolytic effectors and target
      cells. Here, we report the crystal structure of the heterophilic adhesion complex
      between the amino-terminal domains of human CD2 and CD58. A strikingly
      asymmetric, orthogonal, face-to-face interaction involving the major beta sheets 
      of the respective immunoglobulin-like domains with poor shape complementarity is 
      revealed. In the virtual absence of hydrophobic forces, interdigitating charged
      amino acid side chains form hydrogen bonds and salt links at the interface
      (approximately 1200 A2), imparting a high degree of specificity albeit with low
      affinity (K(D) of approximately microM). These features explain CD2-CD58 dynamic 
      binding, offering insights into interactions of related immunoglobulin
      superfamily receptors.
FAU - Wang, J H
AU  - Wang JH
AD  - Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, Massachusetts 
      02115, USA. jwang@red.dfci.harvard.edu
FAU - Smolyar, A
AU  - Smolyar A
FAU - Tan, K
AU  - Tan K
FAU - Liu, J H
AU  - Liu JH
FAU - Kim, M
AU  - Kim M
FAU - Sun, Z Y
AU  - Sun ZY
FAU - Wagner, G
AU  - Wagner G
FAU - Reinherz, E L
AU  - Reinherz EL
LA  - eng
SI  - PDB/1QA9
GR  - AI21226/AI/NIAID NIH HHS/United States
GR  - AI37581/AI/NIAID NIH HHS/United States
GR  - GM56008/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (CD2 Antigens)
RN  - 0 (CD58 Antigens)
RN  - 0 (Cell Adhesion Molecules)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - CD2 Antigens/*chemistry/metabolism
MH  - CD58 Antigens/*chemistry/metabolism
MH  - Cell Adhesion Molecules/chemistry
MH  - Crystallography, X-Ray
MH  - Humans
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Rats
MH  - Sequence Homology, Amino Acid
EDAT- 1999/06/25 00:00
MHDA- 1999/06/25 00:01
CRDT- 1999/06/25 00:00
PHST- 1999/06/25 00:00 [pubmed]
PHST- 1999/06/25 00:01 [medline]
PHST- 1999/06/25 00:00 [entrez]
AID - S0092-8674(00)80790-4 [pii]
AID - 10.1016/s0092-8674(00)80790-4 [doi]
PST - ppublish
SO  - Cell. 1999 Jun 11;97(6):791-803. doi: 10.1016/s0092-8674(00)80790-4.