1epf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1epf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1epf, resolution 1.85&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Line 1: Line 1:
-
[[Image:1epf.gif|left|200px]]<br /><applet load="1epf" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1epf.gif|left|200px]]<br /><applet load="1epf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1epf, resolution 1.85&Aring;" />
caption="1epf, resolution 1.85&Aring;" />
'''CRYSTAL STRUCTURE OF THE TWO N-TERMINAL IMMUNOGLOBULIN DOMAINS OF THE NEURAL CELL ADHESION MOLECULE (NCAM)'''<br />
'''CRYSTAL STRUCTURE OF THE TWO N-TERMINAL IMMUNOGLOBULIN DOMAINS OF THE NEURAL CELL ADHESION MOLECULE (NCAM)'''<br />
==Overview==
==Overview==
-
The neural cell adhesion molecule NCAM, a member of the immunoglobulin, superfamily, mediates cell-cell recognition and adhesion via a homophilic, interaction. NCAM plays a key role during development and regeneration of, the nervous system and is involved in synaptic plasticity associated with, memory and learning. The 1.85 A crystal structure of the two N-terminal, extracellular domains of NCAM reported here provides a structural basis, for the homophilic interaction. The molecular packing of the two-domain, structure reveals a cross shaped antiparallel dimer, and provides, fundamental insight into trans-cellular recognition mediated by NCAM.
+
The neural cell adhesion molecule NCAM, a member of the immunoglobulin superfamily, mediates cell-cell recognition and adhesion via a homophilic interaction. NCAM plays a key role during development and regeneration of the nervous system and is involved in synaptic plasticity associated with memory and learning. The 1.85 A crystal structure of the two N-terminal extracellular domains of NCAM reported here provides a structural basis for the homophilic interaction. The molecular packing of the two-domain structure reveals a cross shaped antiparallel dimer, and provides fundamental insight into trans-cellular recognition mediated by NCAM.
==About this Structure==
==About this Structure==
-
1EPF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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=1EPF OCA].
+
1EPF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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=1EPF OCA].
==Reference==
==Reference==
Line 16: Line 16:
[[Category: Bock, E.]]
[[Category: Bock, E.]]
[[Category: Ikemizu, S.]]
[[Category: Ikemizu, S.]]
-
[[Category: Jones, E.Y.]]
+
[[Category: Jones, E Y.]]
[[Category: Kasper, C.]]
[[Category: Kasper, C.]]
-
[[Category: Kastrup, J.S.]]
+
[[Category: Kastrup, J S.]]
-
[[Category: Larsen, I.K.]]
+
[[Category: Larsen, I K.]]
[[Category: Rasmussen, H.]]
[[Category: Rasmussen, H.]]
[[Category: CA]]
[[Category: CA]]
Line 26: Line 26:
[[Category: ncam]]
[[Category: ncam]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:12:00 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:16 2008''

Revision as of 10:30, 21 February 2008


1epf, resolution 1.85Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE TWO N-TERMINAL IMMUNOGLOBULIN DOMAINS OF THE NEURAL CELL ADHESION MOLECULE (NCAM)

Overview

The neural cell adhesion molecule NCAM, a member of the immunoglobulin superfamily, mediates cell-cell recognition and adhesion via a homophilic interaction. NCAM plays a key role during development and regeneration of the nervous system and is involved in synaptic plasticity associated with memory and learning. The 1.85 A crystal structure of the two N-terminal extracellular domains of NCAM reported here provides a structural basis for the homophilic interaction. The molecular packing of the two-domain structure reveals a cross shaped antiparallel dimer, and provides fundamental insight into trans-cellular recognition mediated by NCAM.

About this Structure

1EPF is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis of cell-cell adhesion by NCAM., Kasper C, Rasmussen H, Kastrup JS, Ikemizu S, Jones EY, Berezin V, Bock E, Larsen IK, Nat Struct Biol. 2000 May;7(5):389-93. PMID:10802736

Page seeded by OCA on Thu Feb 21 12:30:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools