1qa9

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(New page: 200px<br /><applet load="1qa9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qa9, resolution 3.2&Aring;" /> '''Structure of a Hetero...)
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[[Image:1qa9.jpg|left|200px]]<br /><applet load="1qa9" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qa9.jpg|left|200px]]<br /><applet load="1qa9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qa9, resolution 3.2&Aring;" />
caption="1qa9, resolution 3.2&Aring;" />
'''Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors'''<br />
'''Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1QA9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QA9 OCA].
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1QA9 is a [http://en.wikipedia.org/wiki/Protein_complex 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==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Kim, M.]]
[[Category: Kim, M.]]
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[[Category: Liu, J.H.]]
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[[Category: Liu, J H.]]
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[[Category: Reinherz, E.L.]]
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[[Category: Reinherz, E L.]]
[[Category: Smolyar, A.]]
[[Category: Smolyar, A.]]
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[[Category: Sun, Z.J.]]
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[[Category: Sun, Z J.]]
[[Category: Tan, K.]]
[[Category: Tan, K.]]
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
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[[Category: Wang, J.H.]]
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[[Category: Wang, J H.]]
[[Category: cd2]]
[[Category: cd2]]
[[Category: cd58]]
[[Category: cd58]]
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[[Category: ig-like domain]]
[[Category: ig-like domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:31:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:33 2008''

Revision as of 12:37, 21 February 2008

Image:1qa9.jpg

1qa9, resolution 3.2Å

Drag the structure with the mouse to rotate

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

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