1qa9
From Proteopedia
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| - | [[Image:1qa9.jpg|left|200px]] | + | [[Image:1qa9.jpg|left|200px]] |
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| - | '''Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors''' | + | {{Structure |
| + | |PDB= 1qa9 |SIZE=350|CAPTION= <scene name='initialview01'>1qa9</scene>, resolution 3.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QA9 is a [ | + | 1QA9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QA9 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors., Wang JH, Smolyar A, Tan K, Liu JH, Kim M, Sun ZY, Wagner G, Reinherz EL, Cell. 1999 Jun 11;97(6):791-803. PMID:[http:// | + | Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors., Wang JH, Smolyar A, Tan K, Liu JH, Kim M, Sun ZY, Wagner G, Reinherz EL, Cell. 1999 Jun 11;97(6):791-803. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10380930 10380930] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ig-like domain]] | [[Category: ig-like domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:35:01 2008'' |
Revision as of 11:35, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors
Overview
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.
About this Structure
1QA9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors., Wang JH, Smolyar A, Tan K, Liu JH, Kim M, Sun ZY, Wagner G, Reinherz EL, Cell. 1999 Jun 11;97(6):791-803. PMID:10380930
Page seeded by OCA on Thu Mar 20 13:35:01 2008
Categories: Homo sapiens | Protein complex | Kim, M. | Liu, J H. | Reinherz, E L. | Smolyar, A. | Sun, Z J. | Tan, K. | Wagner, G. | Wang, J H. | Cd2 | Cd58 | Cell adhesion | Ig-like domain
