1m31: Difference between revisions

Line 1:

[[Image:1m31.gif|left|200px]]<br />

[[Image:1m31.gif|left|200px]]<br /><applet load="1m31" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1m31" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1m31" />

'''Three-Dimensional Solution Structure of Apo-Mts1'''<br />

==Overview==

Mts1 is a member of the S100 family of Ca2+-binding proteins and is, implicated in promoting tumor progression and metastasis. To better, understand the structure-function relationships of this protein and to, begin characterizing its Ca2+-dependent interaction with protein binding, targets, the three-dimensional structure of mts1 was determined in the apo, state by NMR spectroscopy. As with other S100 protein family members, mts1, is a symmetric homodimer held together by noncovalent interactions between, two helices from each subunit (helices 1, 4, 1', and 4') to form an X-type, four-helix bundle. Each subunit of mts1 has two EF-hand Ca2+-binding, domains: a pseudo-EF-hand (or S100-hand) and a typical EF-hand that are, brought into proximity by a small two-stranded antiparallel beta-sheet., The S100-hand is formed by helices 1 and 2, and is similar in conformation, to other members of the S100 family. In the typical EF-hand, the position, of helix 3 is similar to that of another member of the S100 protein, family, calcyclin (S100A6), and less like that of other S100 family, members for which three-dimensional structures are available in the, calcium-free state (e.g., S100B and S100A1). The differences in the, position of helix 3 in the apo state of these four S100 proteins are, likely due to variations in the amino acid sequence in the C-terminus of, helix 4 and in loop 2 (the hinge region) and could potentially be used to, subclassify the S100 protein family.

Mts1 is a member of the S100 family of Ca2+-binding proteins and is implicated in promoting tumor progression and metastasis. To better understand the structure-function relationships of this protein and to begin characterizing its Ca2+-dependent interaction with protein binding targets, the three-dimensional structure of mts1 was determined in the apo state by NMR spectroscopy. As with other S100 protein family members, mts1 is a symmetric homodimer held together by noncovalent interactions between two helices from each subunit (helices 1, 4, 1', and 4') to form an X-type four-helix bundle. Each subunit of mts1 has two EF-hand Ca2+-binding domains: a pseudo-EF-hand (or S100-hand) and a typical EF-hand that are brought into proximity by a small two-stranded antiparallel beta-sheet. The S100-hand is formed by helices 1 and 2, and is similar in conformation to other members of the S100 family. In the typical EF-hand, the position of helix 3 is similar to that of another member of the S100 protein family, calcyclin (S100A6), and less like that of other S100 family members for which three-dimensional structures are available in the calcium-free state (e.g., S100B and S100A1). The differences in the position of helix 3 in the apo state of these four S100 proteins are likely due to variations in the amino acid sequence in the C-terminus of helix 4 and in loop 2 (the hinge region) and could potentially be used to subclassify the S100 protein family.

==About this Structure==

1M31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1M31 OCA].

1M31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1M31 OCA].

==Reference==

Line 14:

Line 13:

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Bresnick, A.R.]]

[[Category: Bresnick, A R.]]

[[Category: Ellis, K.C.]]

[[Category: Ellis, K C.]]

[[Category: Rustandi, R.R.]]

[[Category: Rustandi, R R.]]

[[Category: Vallely, K.M.]]

[[Category: Vallely, K M.]]

[[Category: Varlamova, O.]]

[[Category: Weber, D.J.]]

[[Category: Weber, D J.]]

[[Category: non-covalent homodimer]]

[[Category: x-type four-helix bundle]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:06:~~34 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:57 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1m31.gif|left|200px]]<br />
+[[Image:1m31.gif|left|200px]]<br /><applet load="1m31" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1m31" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1m31" />
 '''Three-Dimensional Solution Structure of Apo-Mts1'''<br />
 ==Overview==
-Mts1 is a member of the S100 family of Ca2+-binding proteins and is, implicated in promoting tumor progression and metastasis. To better, understand the structure-function relationships of this protein and to, begin characterizing its Ca2+-dependent interaction with protein binding, targets, the three-dimensional structure of mts1 was determined in the apo, state by NMR spectroscopy. As with other S100 protein family members, mts1, is a symmetric homodimer held together by noncovalent interactions between, two helices from each subunit (helices 1, 4, 1', and 4') to form an X-type, four-helix bundle. Each subunit of mts1 has two EF-hand Ca2+-binding, domains: a pseudo-EF-hand (or S100-hand) and a typical EF-hand that are, brought into proximity by a small two-stranded antiparallel beta-sheet., The S100-hand is formed by helices 1 and 2, and is similar in conformation, to other members of the S100 family. In the typical EF-hand, the position, of helix 3 is similar to that of another member of the S100 protein, family, calcyclin (S100A6), and less like that of other S100 family, members for which three-dimensional structures are available in the, calcium-free state (e.g., S100B and S100A1). The differences in the, position of helix 3 in the apo state of these four S100 proteins are, likely due to variations in the amino acid sequence in the C-terminus of, helix 4 and in loop 2 (the hinge region) and could potentially be used to, subclassify the S100 protein family.
+Mts1 is a member of the S100 family of Ca2+-binding proteins and is implicated in promoting tumor progression and metastasis. To better understand the structure-function relationships of this protein and to begin characterizing its Ca2+-dependent interaction with protein binding targets, the three-dimensional structure of mts1 was determined in the apo state by NMR spectroscopy. As with other S100 protein family members, mts1 is a symmetric homodimer held together by noncovalent interactions between two helices from each subunit (helices 1, 4, 1', and 4') to form an X-type four-helix bundle. Each subunit of mts1 has two EF-hand Ca2+-binding domains: a pseudo-EF-hand (or S100-hand) and a typical EF-hand that are brought into proximity by a small two-stranded antiparallel beta-sheet. The S100-hand is formed by helices 1 and 2, and is similar in conformation to other members of the S100 family. In the typical EF-hand, the position of helix 3 is similar to that of another member of the S100 protein family, calcyclin (S100A6), and less like that of other S100 family members for which three-dimensional structures are available in the calcium-free state (e.g., S100B and S100A1). The differences in the position of helix 3 in the apo state of these four S100 proteins are likely due to variations in the amino acid sequence in the C-terminus of helix 4 and in loop 2 (the hinge region) and could potentially be used to subclassify the S100 protein family.
 ==About this Structure==
-M31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1M31 OCA].
+M31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1M31 OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Bresnick, A.R.]]
+[[Category: Bresnick, A R.]]
-[[Category: Ellis, K.C.]]
+[[Category: Ellis, K C.]]
-[[Category: Rustandi, R.R.]]
+[[Category: Rustandi, R R.]]
-[[Category: Vallely, K.M.]]
+[[Category: Vallely, K M.]]
 [[Category: Varlamova, O.]]
-[[Category: Weber, D.J.]]
+[[Category: Weber, D J.]]
 [[Category: non-covalent homodimer]]
 [[Category: x-type four-helix bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:06:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:57 2008''