1mim

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(New page: 200px<br /> <applet load="1mim" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mim, resolution 2.6&Aring;" /> '''IGG FAB FRAGMENT (CD...)
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'''IGG FAB FRAGMENT (CD25-BINDING)'''<br />
'''IGG FAB FRAGMENT (CD25-BINDING)'''<br />
==Overview==
==Overview==
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A specific drug targeted to the IL-2 receptor on activated T lymphocytes, could limit acute immunological rejection during organ transplantation. A, high-affinity monoclonal antibody directed against the alpha-chain of the, IL-2 receptor (CD25) was chimerized with the constant regions of the human, IgG1 heavy and k light chain resulting in SDZ CHII621 [Amlot, Rawlings, Fernando, Griffin, Heinrich, Schreier, Castaigne, Moore &amp; Sweny (1995)., Transplantation, 60, 748-756]. The Fab fragment of SDZ CHI621 has been, purified and crystallized (P2(l), a = 39.58, b = 59.76, c = 102.09 A, beta, = 99.98 degrees ). Its structure has been determined by molecular, replacement and refined at 2.6 A to a crystallographic R factor of 19.7%., The protein exhibits the typical immunoglobulin fold. The complementary, determining regions (CDR's) 1 and 2 of both heavy and light chains show, similar conformations to other known reported structures whereas the CDR3, from the light chain seems to adopt a novel type of conformation. There is, a network of interactions which maintain the CDR3 of both chains together, and limit their solvent accessibility. The interaction between V(L) and, C(L) has been strengthened by the chimerization whereas that between V(H), and C(H)1 has been weakened.
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A specific drug targeted to the IL-2 receptor on activated T lymphocytes could limit acute immunological rejection during organ transplantation. A high-affinity monoclonal antibody directed against the alpha-chain of the IL-2 receptor (CD25) was chimerized with the constant regions of the human IgG1 heavy and k light chain resulting in SDZ CHII621 [Amlot, Rawlings, Fernando, Griffin, Heinrich, Schreier, Castaigne, Moore &amp; Sweny (1995). Transplantation, 60, 748-756]. The Fab fragment of SDZ CHI621 has been purified and crystallized (P2(l), a = 39.58, b = 59.76, c = 102.09 A, beta = 99.98 degrees ). Its structure has been determined by molecular replacement and refined at 2.6 A to a crystallographic R factor of 19.7%. The protein exhibits the typical immunoglobulin fold. The complementary determining regions (CDR's) 1 and 2 of both heavy and light chains show similar conformations to other known reported structures whereas the CDR3 from the light chain seems to adopt a novel type of conformation. There is a network of interactions which maintain the CDR3 of both chains together and limit their solvent accessibility. The interaction between V(L) and C(L) has been strengthened by the chimerization whereas that between V(H) and C(H)1 has been weakened.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1MIM 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=1MIM OCA].
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1MIM 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=1MIM OCA].
==Reference==
==Reference==
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:11:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:30 2008''

Revision as of 11:55, 21 February 2008


1mim, resolution 2.6Å

Drag the structure with the mouse to rotate

IGG FAB FRAGMENT (CD25-BINDING)

Contents

Overview

A specific drug targeted to the IL-2 receptor on activated T lymphocytes could limit acute immunological rejection during organ transplantation. A high-affinity monoclonal antibody directed against the alpha-chain of the IL-2 receptor (CD25) was chimerized with the constant regions of the human IgG1 heavy and k light chain resulting in SDZ CHII621 [Amlot, Rawlings, Fernando, Griffin, Heinrich, Schreier, Castaigne, Moore & Sweny (1995). Transplantation, 60, 748-756]. The Fab fragment of SDZ CHI621 has been purified and crystallized (P2(l), a = 39.58, b = 59.76, c = 102.09 A, beta = 99.98 degrees ). Its structure has been determined by molecular replacement and refined at 2.6 A to a crystallographic R factor of 19.7%. The protein exhibits the typical immunoglobulin fold. The complementary determining regions (CDR's) 1 and 2 of both heavy and light chains show similar conformations to other known reported structures whereas the CDR3 from the light chain seems to adopt a novel type of conformation. There is a network of interactions which maintain the CDR3 of both chains together and limit their solvent accessibility. The interaction between V(L) and C(L) has been strengthened by the chimerization whereas that between V(H) and C(H)1 has been weakened.

Disease

Known disease associated with this structure: Kappa light chain deficiency OMIM:[147200]

About this Structure

1MIM is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the fab fragment of SDZ CHI621: a chimeric antibody against CD25., Mikol V, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):534-42. PMID:15299676

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