1lcj

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[[Image:1lcj.png|left|200px]]
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{{STRUCTURE_1lcj| PDB=1lcj | SCENE= }}
{{STRUCTURE_1lcj| PDB=1lcj | SCENE= }}
===SH2 (SRC HOMOLOGY-2) DOMAIN OF HUMAN P56-LCK TYROSINE KINASE COMPLEXED WITH THE 11 RESIDUE PHOSPHOTYROSYL PEPTIDE EPQPYEEIPIYL===
===SH2 (SRC HOMOLOGY-2) DOMAIN OF HUMAN P56-LCK TYROSINE KINASE COMPLEXED WITH THE 11 RESIDUE PHOSPHOTYROSYL PEPTIDE EPQPYEEIPIYL===
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{{ABSTRACT_PUBMED_7680435}}
{{ABSTRACT_PUBMED_7680435}}
==About this Structure==
==About this Structure==
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1LCJ is a 2 chains 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=1LCJ OCA].
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[[1lcj]] is a 2 chain structure of [[Tyrosine kinase]] with sequence 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=1LCJ OCA].
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==See Also==
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*[[Tyrosine kinase|Tyrosine kinase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:7680435</ref><references group="xtra"/>
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<ref group="xtra">PMID:007680435</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Eck, M.]]
[[Category: Eck, M.]]
[[Category: Harrison, S.]]
[[Category: Harrison, S.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:38:13 2009''
 

Revision as of 14:58, 25 July 2012

Image:1lcj.png

Template:STRUCTURE 1lcj

Contents

SH2 (SRC HOMOLOGY-2) DOMAIN OF HUMAN P56-LCK TYROSINE KINASE COMPLEXED WITH THE 11 RESIDUE PHOSPHOTYROSYL PEPTIDE EPQPYEEIPIYL

Template:ABSTRACT PUBMED 7680435

About this Structure

1lcj is a 2 chain structure of Tyrosine kinase with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Eck MJ, Shoelson SE, Harrison SC. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Nature. 1993 Mar 4;362(6415):87-91. PMID:7680435 doi:http://dx.doi.org/10.1038/362087a0

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