1dyk

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(New page: 200px<br /><applet load="1dyk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dyk, resolution 2.00&Aring;" /> '''LAMININ ALPHA 2 CHAI...)
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[[Image:1dyk.gif|left|200px]]<br /><applet load="1dyk" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dyk, resolution 2.00&Aring;" />
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'''LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR'''<br />
'''LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR'''<br />
==Overview==
==Overview==
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The laminins are large heterotrimeric glycoproteins with fundamental roles, in basement membrane architecture and function. The C-terminus of the, laminin alpha chain contains a tandem of five laminin G-like (LG) domains., We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain, pair, which harbours binding sites for heparin and the cell surface, receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3, fragment. LG4 and LG5 are arranged in a V-shaped fashion related by a 110, degrees rotation about an axis passing near the domain termini. An, extended N-terminal segment is disulfide bonded to LG5 and stabilizes the, domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 A, apart at the tips of the domains opposite the polypeptide termini. An, extensive basic surface region between the calcium sites is proposed to, bind alpha-dystroglycan and heparin. The LG4-LG5 structure was used to, construct a model of the laminin LG1-LG5 tandem and interpret missense, mutations underlying protein S deficiency.
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The laminins are large heterotrimeric glycoproteins with fundamental roles in basement membrane architecture and function. The C-terminus of the laminin alpha chain contains a tandem of five laminin G-like (LG) domains. We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3 fragment. LG4 and LG5 are arranged in a V-shaped fashion related by a 110 degrees rotation about an axis passing near the domain termini. An extended N-terminal segment is disulfide bonded to LG5 and stabilizes the domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 A apart at the tips of the domains opposite the polypeptide termini. An extensive basic surface region between the calcium sites is proposed to bind alpha-dystroglycan and heparin. The LG4-LG5 structure was used to construct a model of the laminin LG1-LG5 tandem and interpret missense mutations underlying protein S deficiency.
==About this Structure==
==About this Structure==
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1DYK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DYK OCA].
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1DYK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYK OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Hohenester, E.]]
[[Category: Hohenester, E.]]
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[[Category: Talts, J.F.]]
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[[Category: Talts, J F.]]
[[Category: Timple, R.]]
[[Category: Timple, R.]]
[[Category: Tisi, D.]]
[[Category: Tisi, D.]]
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[[Category: laminin]]
[[Category: laminin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:41:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:54 2008''

Revision as of 10:21, 21 February 2008

Image:1dyk.gif

1dyk, resolution 2.00Å

Drag the structure with the mouse to rotate

LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR

Overview

The laminins are large heterotrimeric glycoproteins with fundamental roles in basement membrane architecture and function. The C-terminus of the laminin alpha chain contains a tandem of five laminin G-like (LG) domains. We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3 fragment. LG4 and LG5 are arranged in a V-shaped fashion related by a 110 degrees rotation about an axis passing near the domain termini. An extended N-terminal segment is disulfide bonded to LG5 and stabilizes the domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 A apart at the tips of the domains opposite the polypeptide termini. An extensive basic surface region between the calcium sites is proposed to bind alpha-dystroglycan and heparin. The LG4-LG5 structure was used to construct a model of the laminin LG1-LG5 tandem and interpret missense mutations underlying protein S deficiency.

About this Structure

1DYK is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin., Tisi D, Talts JF, Timpl R, Hohenester E, EMBO J. 2000 Apr 3;19(7):1432-40. PMID:10747011

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